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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR011859 | 11,859 | Dihydrodipicolinate reductase, plant-type | Dihydrodipicolinate_Rdtase_pln | Family | 871 | false | false | Dihydrodipicolinate reductase is an enzyme found in bacteria and higher plants which is involved in the biosynthesis of diaminopimelic acid, a component of bacterial cell walls, and the essential amino acid L-lysine. It catalyses the the reduced pyridine nucleotide-dependent reduction of the alpha,beta-unsaturated cycl... | [
"GO:0008839",
"GO:0070402",
"GO:0009089"
] | [
"4-hydroxy-tetrahydrodipicolinate reductase activity",
"NADPH binding",
"L-lysine biosynthetic process via diaminopimelate"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02130"
] | [
"dapB_plant"
] | [
871
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.17.1.8",
"GenProp0125",
"PWY-2941",
"PWY-2942",
"PWY-5097"
] | [
"EC:1.17.1.8",
"GP:GenProp0125",
"METACYC:PWY-2941",
"METACYC:PWY-2942",
"METACYC:PWY-5097"
] | 5 | [
"5u5i",
"5u5n",
"5ua0",
"7t34"
] | 4 | [
"PUB00028085"
] | [
"8993314"
] | [
"Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy."
] | [
1997
] | 1 | [
"IPR023940"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
39,
832
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
7,
3,
10
] | 3 | true | Family | Dihydrodipicolinate reductase, plant-type | Dihydrodipicolinate reductase, plant-type | Dihydrodipicolinate_Rdtase_pln | 2 |
IPR011860 | 11,860 | Ribose 5-phosphate isomerase B, Actinobacteria-type | Rib-5-P_Isoase_Actino | Family | 6,486 | false | false | This family is a member of the RpiB/LacA/LacB family. It includes ribose 5-phosphate isomerases and D-erythrulose-4-phosphate isomerases [ ]. The only candidates for ribose 5-phosphate isomerase in the Actinobacteria are members of this family [ , ]. Ribose 5-phosphate isomerase ( ) forms a homodimer and catalyses the ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02133"
] | [
"RPI_actino"
] | [
6486
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"5.3.1.6",
"GenProp0120",
"PWY-1861",
"PWY-5723",
"PWY-8178"
] | [
"EC:5.3.1.6",
"GP:GenProp0120",
"METACYC:PWY-1861",
"METACYC:PWY-5723",
"METACYC:PWY-8178"
] | 5 | [
"1usl",
"2bes",
"2bet",
"2vvo",
"2vvp",
"2vvq",
"3qd5",
"3sdw",
"3sgw"
] | 9 | [
"PUB00031889",
"PUB00049924",
"PUB00091680"
] | [
"14687575",
"18640127",
"26560079"
] | [
"Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site.",
"D-ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase, while the Mycobacterium tuberculosis enzyme is not.",
"A General Strategy for the Discovery of Metabo... | [
2004,
2008,
2015
] | 3 | [
"IPR003500"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"metagenomes"
] | [
5315,
2,
1057,
112
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)"
] | [
1
] | 1 | true | Family | Ribose 5-phosphate isomerase B, Actinobacteria-type | Ribose 5-phosphate isomerase B, Actinobacteria-type | Rib-5-P_Isoase_Actino | 9 |
IPR011861 | 11,861 | Transaldolase, Staphylococcus-type | Transald_staph-type | Family | 560 | false | false | This small family of proteins belong to the transaldolases. Coxiella and Staphylococcus lack members of the known transaldolase families and appear to require a transaldolase activity for completion of the pentose phosphate pathway. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02134"
] | [
"transald_staph"
] | [
560
] | 1 | [
"GP"
] | [
"GenProp0120"
] | [
"GP:GenProp0120"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR033919"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanomicrobiales",
"metagenomes",
"uncultured Caudovirales phage"
] | [
544,
3,
12,
1
] | 4 | [] | [] | 0 | true | Family | Transaldolase, Staphylococcus-type | Transaldolase, Staphylococcus-type | Transald_staph-type | 5 |
IPR011862 | 11,862 | Phosphate binding protein | Phos-bd | Family | 11,400 | false | false | Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons [ , ]. This entry separates members from the phosphate ABC transporter phosphate binding proteins described by . | [
"GO:0042301"
] | [
"phosphate ion binding"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02136"
] | [
"ptsS_2"
] | [
11400
] | 1 | [
"GP"
] | [
"GenProp0190"
] | [
"GP:GenProp0190"
] | 1 | [
"1twy",
"4ecf",
"4exl",
"4gd5",
"4jwo",
"4lat",
"4omb",
"4pqj",
"4q8r"
] | 9 | [
"PUB00087522",
"PUB00087523"
] | [
"7885237",
"6436026"
] | [
"The SphX protein of Synechococcus species PCC 7942 belongs to a family of phosphate-binding proteins.",
"Phosphate transport in Pseudomonas aeruginosa. Involvement of a periplasmic phosphate-binding protein."
] | [
1994,
1984
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctk4d14",
"metagenomes"
] | [
637,
10652,
15,
1,
95
] | 5 | [] | [] | 0 | true | Family | Phosphate binding protein | Phosphate binding protein | Phos-bd | 6 |
IPR011863 | 11,863 | Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein | HSK-PSP | Family | 1,791 | false | false | This protein is has been characterised as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase [ ]. In Pseudomonas aeruginosa, where the characterisation was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes nei... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02137"
] | [
"HSK-PSP"
] | [
1791
] | 1 | [
"GP"
] | [
"GenProp0159"
] | [
"GP:GenProp0159"
] | 1 | [
"1rku",
"1rkv"
] | 2 | [
"PUB00015488"
] | [
"14699121"
] | [
"The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctnFo11",
"unclassified sequences"
] | [
6,
1720,
3,
1,
61
] | 5 | [] | [] | 0 | true | Family | Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein | Phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein | HSK-PSP | 6 |
IPR011864 | 11,864 | Phosphate ABC transporter, permease protein PstC | Phosphate_PstC | Family | 23,606 | 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... | [
"GO:0005315",
"GO:0006817",
"GO:0016020"
] | [
"phosphate transmembrane transporter activity",
"phosphate ion transport",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02138"
] | [
"phosphate_pstC"
] | [
23606
] | 1 | [
"GP"
] | [
"GenProp0190"
] | [
"GP:GenProp0190"
] | 1 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270"
] | [
"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
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1034,
22163,
19,
390
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phosphate ABC transporter, permease protein PstC | Phosphate ABC transporter, permease protein PstC | Phosphate_PstC | 3 |
IPR011865 | 11,865 | Sulphate ABC transporter, permease protein CysT | CysT_permease | Family | 9,523 | false | false | This entry represents CysT, one of two homologous, tandem permeases in the sulphate ABC transporter system; the other is CysW ( ). The sulphate transporter has been described in Escherichia coli as transporting sulphate, thiosulphate, selenate, and selenite. Sulphate transporters may also transport molybdate ion if a s... | [
"GO:0015419",
"GO:1902358",
"GO:0005886"
] | [
"ABC-type sulfate transporter activity",
"sulfate transmembrane transport",
"plasma membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02139"
] | [
"permease_CysT"
] | [
9523
] | 1 | [
"GP"
] | [
"GenProp0191"
] | [
"GP:GenProp0191"
] | 1 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270"
] | [
"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
] | 11 | [
"IPR005667"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
9283,
210,
30
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Sulphate ABC transporter, permease protein CysT | Sulphate ABC transporter, permease protein CysT | CysT_permease | 5 |
IPR011866 | 11,866 | Sulphate ABC transporter, permease protein CysW | CysW_permease | Family | 8,648 | false | false | This entry represents CysW, one of two homologous, tandem permeases in the sulphate ABC transporter system; the other is CysT ( ). The sulphate transporter has been described in Escherichia coli as transporting sulphate, thiosulphate, selenate, and selenite. Sulphate transporters may also transport molybdate ion if a s... | [
"GO:0005886"
] | [
"plasma membrane"
] | [
"cellular_component"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02140"
] | [
"permease_CysW"
] | [
8648
] | 1 | [
"GP"
] | [
"GenProp0191"
] | [
"GP:GenProp0191"
] | 1 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270"
] | [
"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
] | 11 | [
"IPR005667"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
8580,
46,
22
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Sulphate ABC transporter, permease protein CysW | Sulphate ABC transporter, permease protein CysW | CysW_permease | 7 |
IPR011868 | 11,868 | Molybdate ABC transporter, ATP-binding protein | ModC_ABC_ATP-bd | Family | 6,575 | 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... | [
"GO:0005524",
"GO:0015098",
"GO:0140359",
"GO:0015689",
"GO:0016020"
] | [
"ATP binding",
"molybdate ion transmembrane transporter activity",
"ABC-type transporter activity",
"molybdate ion transport",
"membrane"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 5 | [
"NCBIFAM"
] | [
"TIGR02142"
] | [
"modC_ABC"
] | [
6575
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"7.3.2.5",
"GenProp0192",
"PWY-8171"
] | [
"EC:7.3.2.5",
"GP:GenProp0192",
"METACYC:PWY-8171"
] | 3 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270"
] | [
"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
] | 11 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Sym plasmid",
"unclassified sequences"
] | [
6500,
7,
1,
67
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Molybdate ABC transporter, ATP-binding protein | Molybdate ABC transporter, ATP-binding protein | ModC_ABC_ATP-bd | 2 |
IPR011869 | 11,869 | tRNA/tmRNA (uracil-C(5))-methyltransferase, TrmA | TrmA_MeTrfase | Family | 5,025 | false | false | This family consists of methyltransferases. The family member from Escherichia coli has been shown to have dual-specificity, catalysing the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA) [ , , ]. This enzyme is inhibited by adenosylhomocystei... | [
"GO:0030697",
"GO:0006396"
] | [
"tRNA (uracil(54)-C5)-methyltransferase activity, S-adenosyl methionine-dependent",
"RNA processing"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_01011",
"PTHR47790",
"TIGR02143"
] | [
"RNA_methyltr_TrmA",
"",
"trmA_only"
] | [
4643,
5025,
4667
] | 3 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"... | [
"2.1.1.-",
"2.1.1.35",
"PWY-1061",
"PWY-2083",
"PWY-3542",
"PWY-4021",
"PWY-4161",
"PWY-4202",
"PWY-5059",
"PWY-5105",
"PWY-5301",
"PWY-5305",
"PWY-5479",
"PWY-5665",
"PWY-5729",
"PWY-5748",
"PWY-5765",
"PWY-5773",
"PWY-5846",
"PWY-5883",
"PWY-5975",
"PWY-5987",
"PWY-601"... | [
"EC:2.1.1.-",
"EC:2.1.1.35",
"METACYC:PWY-1061",
"METACYC:PWY-2083",
"METACYC:PWY-3542",
"METACYC:PWY-4021",
"METACYC:PWY-4161",
"METACYC:PWY-4202",
"METACYC:PWY-5059",
"METACYC:PWY-5105",
"METACYC:PWY-5301",
"METACYC:PWY-5305",
"METACYC:PWY-5479",
"METACYC:PWY-5665",
"METACYC:PWY-5729",... | 147 | [
"3bt7"
] | 1 | [
"PUB00043357",
"PUB00043359",
"PUB00068774",
"PUB00068775"
] | [
"2999071",
"391549",
"6247318",
"23603891"
] | [
"Genetic organization and transcription from the gene (trmA) responsible for synthesis of tRNA (uracil-5)-methyltransferase by Escherichia coli.",
"Escherichia coli tRNA (uracil-5-)-methyltransferase: Inhibition by analogues of adenosylhomocysteine.",
"Cloning and restriction mapping of the trmA gene coding for... | [
1985,
1979,
1980,
2013
] | 4 | [
"IPR010280"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4750,
241,
34
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | tRNA/tmRNA (uracil-C(5))-methyltransferase, TrmA | tRNA/tmRNA (uracil-C(5))-methyltransferase, TrmA | TrmA_MeTrfase | 1 |
IPR011870 | 11,870 | Lysine biosynthesis enzyme LysX | LysX_arch | Family | 987 | false | false | The family of proteins found in this family include the characterised LysX from Thermus thermophilus [ ] which is part of a well-organised lysine biosynthesis gene cluster [ ]. LysX is believed to carry out an ATP-dependent acylation of the amino group of alpha-aminoadipate in the prokaryotic version of the fungal AAA ... | [
"GO:0003824",
"GO:0005524",
"GO:0009085"
] | [
"catalytic activity",
"ATP binding",
"L-lysine biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02144"
] | [
"LysX_arch"
] | [
987
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"6.3.2.43",
"GenProp0193",
"PWY-3081"
] | [
"EC:6.3.2.43",
"GP:GenProp0193",
"METACYC:PWY-3081"
] | 3 | [
"1uc8",
"1uc9",
"3vpb",
"3vpc",
"3vpd",
"5k2m"
] | 6 | [
"PUB00015489",
"PUB00015490",
"PUB00015491"
] | [
"12963379",
"10613839",
"2570347"
] | [
"Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8.",
"A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis.",
"Characterization of the gene rimK responsible for the addition of glutam... | [
2003,
1999,
1989
] | 3 | [
"IPR004666"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Geodia barretti",
"unclassified sequences"
] | [
650,
315,
2,
20
] | 4 | [] | [] | 0 | true | Family | Lysine biosynthesis enzyme LysX | Lysine biosynthesis enzyme LysX | LysX_arch | 9 |
IPR011871 | 11,871 | Fibrobacter succinogenes major paralogous domain | Fib_succ_major | Domain | 2,241 | false | false | This domain of about 175 to 200 amino acids is found, in from one to five copies, in over 50 proteins in Fibrobacter succinogenes, an obligate anaerobe of the rumen. Many members of this family have an apparent lipoprotein signal sequence. Conserved cysteine residues, suggestive of disulphide bond formation, are also c... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF09603",
"TIGR02145"
] | [
"Fib_succ_major",
"Fib_succ_major"
] | [
2158,
1964
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"metagenomes"
] | [
2153,
4,
4,
80
] | 4 | [] | [] | 0 | true | Domain | Fibrobacter succinogenes major paralogous domain | Fibrobacter succinogenes major paralogous domain | Fib_succ_major | 4 |
IPR011872 | 11,872 | Homocitrate synthase | Homocitrate_synth | Family | 2,147 | false | false | This entry includes the yeast LYS21 gene which carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway [ , ]. A related pathway is found in Thermus thermophilus [ ]. This enzyme is closely related to 2-isopropylmalate synthase (LeuA) and citramalate synthase (CimA), both of which are pres... | [
"GO:0004410",
"GO:0046912",
"GO:0019752",
"GO:0019878"
] | [
"homocitrate synthase activity",
"acyltransferase activity, acyl groups converted into alkyl on transfer",
"carboxylic acid metabolic process",
"L-lysine biosynthetic process via aminoadipic acid"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_02222",
"TIGR02146"
] | [
"Homocitr_synth_fung_arch",
"LysS_fung_arch"
] | [
1990,
2123
] | 2 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"2.3.3.14",
"GenProp0193",
"PWY-3081",
"PWY-7710"
] | [
"EC:2.3.3.14",
"GP:GenProp0193",
"METACYC:PWY-3081",
"METACYC:PWY-7710"
] | 4 | [
"2ztj",
"2ztk",
"2zyf",
"3a9i",
"3ivs",
"3ivt",
"3ivu",
"3mi3",
"6ktq"
] | 9 | [
"PUB00015475",
"PUB00015490",
"PUB00063143",
"PUB00063144"
] | [
"9665716",
"10613839",
"16299000",
"9099739"
] | [
"Alpha-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic Archaea.",
"A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis.",
"Inactiv... | [
1998,
1999,
2006,
1997
] | 4 | [
"IPR050073"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"marine metagenome"
] | [
96,
153,
1897,
1
] | 4 | [
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)"
] | [
1,
2,
1
] | 3 | true | Family | Homocitrate synthase | Homocitrate synthase | Homocitrate_synth | 2 |
IPR011873 | 11,873 | Conserved hypothetical protein CHP02147 | CHP02147 | Family | 353 | false | false | This family consists of members of a paralogous protein family in the rumen anaerobe Fibrobacter succinogenes S85, and a smaller number in Bdellovibrio bacteriovorus HD100. Member proteins are about 270 residues long and appear to lack signal sequences and transmembrane helices. The only perfectly conserved residue is ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02147"
] | [
"Fsuc_second"
] | [
353
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"uncultured microorganism"
] | [
351,
2
] | 2 | [] | [] | 0 | true | Family | Conserved hypothetical protein CHP02147 | Conserved hypothetical protein CHP02147 | CHP02147 | 1 |
IPR011874 | 11,874 | Fibro-slime | Fibro_Slime | Domain | 755 | false | false | This entry represents a conserved region of about 90 amino acids, shared in at least 4 distinct large putative proteins from the slime mold Dictyostelium discoideum (Slime mold) and 10 proteins from the rumen bacterium Fibrobacter succinogenes (Bacteroides succinogenes), and in no other species so far. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02148"
] | [
"Fibro_Slime"
] | [
755
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Nitrososphaerota",
"metagenomes"
] | [
586,
163,
4,
2
] | 4 | [] | [] | 0 | true | Domain | Fibro-slime | Fibro-slime | Fibro_Slime | 1 |
IPR011875 | 11,875 | Alpha-maltose-1-phosphate synthase | M1P_synthase | Family | 3,809 | false | false | Alpha-glucan in mycobacteria is assembled intracellularly utilizing the building block alpha-maltose-1-phosphate (M1P). Mycobacterial GlgA was believed to be a glycogen synthase, but subsequent studies have shown that this enzyme is a M1P-producing glucosyltransferase, producing little or no classical glycogen in vivo.... | [
"GO:0016740",
"GO:0009250"
] | [
"transferase activity",
"glucan biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02149"
] | [
"glgA_Coryne"
] | [
3809
] | 1 | [
"EC",
"METACYC"
] | [
"2.4.1.342",
"PWY-7900"
] | [
"EC:2.4.1.342",
"METACYC:PWY-7900"
] | 2 | [
"6tvp"
] | 1 | [
"PUB00083891"
] | [
"27513637"
] | [
"Metabolic Network for the Biosynthesis of Intra- and Extracellular α-Glucans Required for Virulence of Mycobacterium tuberculosis."
] | [
2016
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
3730,
79
] | 2 | [] | [] | 0 | true | Family | Alpha-maltose-1-phosphate synthase | Alpha-maltose-1-phosphate synthase | M1P_synthase | 1 |
IPR011877 | 11,877 | Ribokinase | Ribokinase | Family | 27,196 | false | false | This entry describes ribokinase enzyme. Ribokinase catalyses the first step in ribose catabolism. This phosphorylation of ribose to ribose-5-phosphate using ATP traps ribose within the cell after uptake and prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphat... | [
"GO:0004747",
"GO:0006014"
] | [
"ribokinase activity",
"D-ribose metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"CDD"
] | [
"MF_01987",
"cd01174"
] | [
"Ribokinase",
"ribokinase"
] | [
26114,
26363
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.1.15",
"R-DDI-71336",
"R-HSA-71336",
"R-MMU-71336",
"R-SCE-71336",
"R-SPO-71336"
] | [
"EC:2.7.1.15",
"REACTOME:R-DDI-71336",
"REACTOME:R-HSA-71336",
"REACTOME:R-MMU-71336",
"REACTOME:R-SCE-71336",
"REACTOME:R-SPO-71336"
] | 6 | [
"1gqt",
"1rk2",
"1rka",
"1rkd",
"1rks",
"1vm7",
"2fv7",
"3go6",
"3go7",
"3i3y",
"3ikh",
"3ry7",
"4x8f",
"4xck",
"4xda",
"5byc",
"5byd",
"5bye",
"5byf",
"5c3y",
"5c3z",
"5c40",
"5c41",
"5zwy",
"6a8a",
"6a8b",
"6a8c",
"6cw5",
"6ilr",
"6ils",
"6ilt",
"6whj"... | 40 | [
"PUB00030699",
"PUB00078860"
] | [
"10438599",
"25084391"
] | [
"Induced fit on sugar binding activates ribokinase.",
"Crystallization and preliminary X-ray analysis of a ribokinase from Vibrio cholerae O395."
] | [
1999,
2014
] | 2 | [
"IPR002139"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
117,
22224,
4660,
195
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",... | [
5,
1,
1,
2,
1,
1,
1,
1,
3,
3,
1,
1,
3
] | 13 | true | Family | Ribokinase | Ribokinase | Ribokinase | 5 |
IPR011879 | 11,879 | Signal transduction response regulator, phosphate regulon transcriptional regulatory protein PhoB | Sig_transdc_resp-reg_PhoB | Family | 7,845 | false | false | Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions [ ]. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk [ ]. These pathways have been adapt... | [
"GO:0000156",
"GO:0003677",
"GO:0000160",
"GO:0006817"
] | [
"phosphorelay response regulator activity",
"DNA binding",
"phosphorelay signal transduction system",
"phosphate ion transport"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"NCBIFAM"
] | [
"TIGR02154"
] | [
"PhoB"
] | [
7845
] | 1 | [
"GP"
] | [
"GenProp0190"
] | [
"GP:GenProp0190"
] | 1 | [] | 0 | [
"PUB00010651",
"PUB00011096",
"PUB00015493",
"PUB00042804",
"PUB00042805",
"PUB00042806",
"PUB00042807"
] | [
"12372152",
"10966457",
"3537313",
"16176121",
"18076326",
"11934609",
"11489844"
] | [
"Histidine protein kinases: key signal transducers outside the animal kingdom.",
"Two-component signal transduction.",
"Nucleotide sequence of the phoB gene, the positive regulatory gene for the phosphate regulon of Escherichia coli K-12.",
"Two-component signal transduction pathways regulating growth and cel... | [
2002,
2000,
1986,
2005,
2007,
2002,
2001
] | 7 | [
"IPR039420"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences",
"uncultured marine group II/III euryarchaeote KM3_133_F10"
] | [
7771,
10,
63,
1
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Signal transduction response regulator, phosphate regulon transcriptional regulatory protein PhoB | Signal transduction response regulator, phosphate regulon transcriptional regulatory protein PhoB | Sig_transdc_resp-reg_PhoB | 6 |
IPR011880 | 11,880 | Phenylacetate-CoA ligase | PA_CoA_ligase | Family | 9,658 | false | false | This entry represents Phenylacetate-coenzyme A ligase (PaaK) found mainly in bacteria and archaea. Phenylacetate-CoA ligase (PA-CoA ligase) catalyses the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA) [ ]. Often located in a conserved gene cluster with enzymes involved in phe... | [
"GO:0047475",
"GO:0010124"
] | [
"phenylacetate-CoA ligase activity",
"phenylacetate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"PIRSF",
"CDD"
] | [
"PIRSF006444",
"cd05913"
] | [
"PaaK",
"PaaK"
] | [
9119,
9654
] | 2 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"6.2.1.30",
"PWY-1341",
"PWY-6318",
"PWY-7716"
] | [
"EC:6.2.1.30",
"METACYC:PWY-1341",
"METACYC:PWY-6318",
"METACYC:PWY-7716"
] | 4 | [
"2y27",
"2y4n",
"2y4o",
"4r1l",
"4r1m",
"4rvn",
"4rvo"
] | 7 | [
"PUB00010200",
"PUB00015494",
"PUB00015495"
] | [
"9748275",
"11260461",
"10629172"
] | [
"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.",
"The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications.",
"Biochemical and molecular characterization of phenylacetate-coenzyme A ligase, an enzyme catalyzing the... | [
1998,
2001,
2000
] | 3 | [] | [
"IPR049623"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
795,
8751,
5,
107
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phenylacetate-CoA ligase | Phenylacetate-CoA ligase | PA_CoA_ligase | 3 |
IPR011881 | 11,881 | 1,2-phenylacetyl-CoA epoxidase, subunit A | PaaA | Family | 6,851 | false | false | This entry represents 1,2-phenylacetyl-CoA epoxidase, subunit A (also known as PaaA). E. coli PaaA and PaaC are components of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyses the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. PaaA is the catalytic subunit involved i... | [
"GO:0097266",
"GO:0010124"
] | [
"phenylacetyl-CoA 1,2-epoxidase activity",
"phenylacetate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02156"
] | [
"PA_CoA_Oxy1"
] | [
6851
] | 1 | [] | [] | [] | 0 | [
"3pvr",
"3pvt",
"3pvy",
"3pw1",
"3pw8",
"3pwq",
"4ii4",
"4iit"
] | 8 | [
"PUB00055817",
"PUB00075378"
] | [
"21247899",
"20660314"
] | [
"Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex.",
"Bacterial phenylalanine and phenylacetate catabolic pathway revealed."
] | [
2011,
2010
] | 2 | [
"IPR007814"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
6683,
3,
123,
42
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 1,2-phenylacetyl-CoA epoxidase, subunit A | 1,2-phenylacetyl-CoA epoxidase, subunit A | PaaA | 5 |
IPR011882 | 11,882 | 1,2-phenylacetyl-CoA epoxidase, subunit C | PaaC | Family | 7,049 | false | false | This entry represents 1,2-phenylacetyl-CoA epoxidase, subunit C (also known as PaaC). E. coli PaaA and PaaC are components of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyses the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. PaaC may be essential for structural int... | [
"GO:0010124"
] | [
"phenylacetate catabolic process"
] | [
"biological_process"
] | 1 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF037834",
"TIGR02158"
] | [
"PA_CoA_Oase3",
"PA_CoA_Oxy3"
] | [
6121,
7048
] | 2 | [] | [] | [] | 0 | [
"1otk",
"3pvr",
"3pvt",
"3pvy",
"3pw1",
"3pw8",
"3pwq",
"4ii4",
"4iit"
] | 9 | [
"PUB00055817",
"PUB00075378"
] | [
"21247899",
"20660314"
] | [
"Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex.",
"Bacterial phenylalanine and phenylacetate catabolic pathway revealed."
] | [
2011,
2010
] | 2 | [
"IPR007814"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"unclassified sequences"
] | [
6848,
4,
154,
43
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 1,2-phenylacetyl-CoA epoxidase, subunit C | 1,2-phenylacetyl-CoA epoxidase, subunit C | PaaC | 8 |
IPR011883 | 11,883 | 1,2-phenylacetyl-CoA epoxidase, subunit D | PaaD-like | Family | 6,768 | false | false | This entry represents the 1,2-phenylacetyl-CoA epoxidase, subunit D (also know as PaaD) and related bacterial proteins. PaaD ia a component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyses the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit D may have ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02159"
] | [
"PA_CoA_Oxy4"
] | [
6768
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005820",
"PUB00010200",
"PUB00153012"
] | [
"9600981",
"9748275",
"16997993"
] | [
"Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: the phenylacetyl-CoA catabolon.",
"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.",
"Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the ... | [
1998,
1998,
2006
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
6720,
3,
45
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 1,2-phenylacetyl-CoA epoxidase, subunit D | 1,2-phenylacetyl-CoA epoxidase, subunit D | PaaD-like | 8 |
IPR011884 | 11,884 | 1,2-phenylacetyl-CoA epoxidase, subunit E | PaaE | Family | 4,696 | false | false | This entry represents the 1,2-phenylacetyl-CoA epoxidase, subunit E (also know as PaaE) and related bacterial proteins. PaaE ia a component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyses the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit E is a redu... | [
"GO:0010124"
] | [
"phenylacetate catabolic process"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02160"
] | [
"PA_CoA_Oxy5"
] | [
4696
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00005820",
"PUB00010200",
"PUB00055817"
] | [
"9600981",
"9748275",
"21247899"
] | [
"Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: the phenylacetyl-CoA catabolon.",
"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.",
"Structural and functional studies of the Escherichia coli phenylacetyl-CoA ... | [
1998,
1998,
2011
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
4675,
2,
19
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 1,2-phenylacetyl-CoA epoxidase, subunit E | 1,2-phenylacetyl-CoA epoxidase, subunit E | PaaE | 8 |
IPR011885 | 11,885 | Periplasmic nitrate reductase c-type cytochrome, NapC/NirT | NO3Rdtase_cyt_c_NapC/NirT | Family | 1,889 | false | false | This entry contains NapC, a predicted membrane-anchored four-heme c-type cytochrome that forms one component of the periplasmic nitrate reductase along with NapA, NapB, NapD, NapE, and NapF subunits. A single known exception at this time is NirT, which is instead a component of a nitrite reductase. This family excludes... | [
"GO:0020037",
"GO:0019333",
"GO:0016020"
] | [
"heme binding",
"denitrification pathway",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02161"
] | [
"napC_nirT"
] | [
1889
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015496"
] | [
"8730872"
] | [
"Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases."
] | [
1996
] | 1 | [
"IPR024717"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"ecological metagenomes"
] | [
1885,
2,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Periplasmic nitrate reductase c-type cytochrome, NapC/NirT | Periplasmic nitrate reductase c-type cytochrome, NapC/NirT | NO3Rdtase_cyt_c_NapC/NirT | 6 |
IPR011886 | 11,886 | Ferredoxin-type protein, NapH/MauN family | NapH_MauN | Family | 2,114 | false | false | Most members of this family are the NapH protein, found next to NapG in operons that encode the periplasmic nitrate reductase [ , ]. Some species with this reductase lack NapC but accomplish electron transfer to NapAB in some other manner, likely to involve NapH, NapG, and/or some other protein. A few members of this p... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02163"
] | [
"napH_"
] | [
2114
] | 1 | [
"GP"
] | [
"GenProp1504"
] | [
"GP:GenProp1504"
] | 1 | [] | 0 | [
"PUB00007706",
"PUB00088159",
"PUB00088160"
] | [
"9202457",
"14674886",
"11967083"
] | [
"Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum ' KT and analysis of mau mutants.",
"NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing.",
"Roles of NapF, NapG and... | [
1997,
2004,
2002
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
2079,
2,
33
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Ferredoxin-type protein, NapH/MauN family | Ferredoxin-type protein, NapH/MauN family | NapH_MauN | 2 |
IPR011887 | 11,887 | Trimethylamine-N-oxide reductase TorA | TorA | Family | 1,402 | false | false | This very narrowly defined family represents trimethylamine-N-oxide (TMAO) reductase TorA. TorA typically is located in the periplasm, has a Tat (twin-arginine translocation)-dependent signal sequence, and is encoded in a torCAD operon. TorA reduces TMAO into trimethylamine; an anaerobic reaction coupled to energy-yiel... | [
"GO:0030151",
"GO:0050626",
"GO:0042597"
] | [
"molybdenum ion binding",
"trimethylamine-N-oxide reductase (cytochrome c) activity",
"periplasmic space"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02164"
] | [
"torA"
] | [
1402
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"GP"
] | [
"1.7.2.3",
"GenProp1205",
"GenProp1341",
"GenProp1535",
"GenProp1582"
] | [
"EC:1.7.2.3",
"GP:GenProp1205",
"GP:GenProp1341",
"GP:GenProp1535",
"GP:GenProp1582"
] | 5 | [
"1tmo",
"9h4t"
] | 2 | [
"PUB00003854",
"PUB00028092"
] | [
"8022286",
"9813127"
] | [
"TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon.",
"Molecular analysis of the trimethylamine N-oxide (TMAO) reductase respiratory system from a Shewanella species."
] | [
1994,
1998
] | 2 | [
"IPR006658"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
1402
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Trimethylamine-N-oxide reductase TorA | Trimethylamine-N-oxide reductase TorA | TorA | 3 |
IPR011888 | 11,888 | Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE | Anaer_DMSO_reductase | Family | 6,492 | false | false | Many bacterial species are capable of anaerobic growth by using dimethylsulphoxide (DMSO) as the terminal electron acceptor, with DMSO reductase as the terminal elctron transfer enzyme. In Escherichia coli and many other Gram-negative bacteria DMSO reductase is a membrane-bound enzyme composed of three subunits; a cata... | [
"GO:0009389",
"GO:0030151",
"GO:0051539"
] | [
"dimethyl sulfoxide reductase activity",
"molybdenum ion binding",
"4 iron, 4 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02166"
] | [
"dmsA_ynfE"
] | [
6492
] | 1 | [
"GP",
"GP"
] | [
"GenProp0637",
"GenProp1148"
] | [
"GP:GenProp0637",
"GP:GenProp1148"
] | 2 | [] | 0 | [
"PUB00028090",
"PUB00034652",
"PUB00034653"
] | [
"16221580",
"1324728",
"14522592"
] | [
"Microbial dimethylsulfoxide and trimethylamine-N-oxide respiration.",
"Molecular analysis of dimethylsulfoxide reductase: a complex iron-sulfur molybdoenzyme of Escherichia coli.",
"The Escherichia coli ynfEFGHI operon encodes polypeptides which are paralogues of dimethyl sulfoxide reductase (DmsABC)."
] | [
2005,
1992,
2003
] | 3 | [] | [
"IPR049754"
] | 0 | 1 | 0 | [
"Bacteria",
"Beauveria bassiana D1-5",
"Escherichia phage RCS47",
"metagenomes"
] | [
6485,
1,
1,
5
] | 4 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Family | Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE | Anaerobic dimethyl sulphoxide reductase, subunit A, DmsA/YnfE | Anaer_DMSO_reductase | 7 |
IPR011889 | 11,889 | Bacterial surface protein 26-residue repeat | Liste_lipo_26 | Repeat | 7,101 | false | false | This entry describes a tandem peptide repeat sequence of 25 or 26 residues, found in predicted surface proteins (often lipoproteins) mainly from Listeria monocytogenes, Listeria innocua, Enterococcus faecalis (Streptococcus faecalis), Lactobacillus plantarum, Mycoplasma spp., Helicobacter hepaticus, and other species. ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02167"
] | [
"Liste_lipo_26"
] | [
7101
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00159277"
] | [
"20626840"
] | [
"A versatile palindromic amphipathic repeat coding sequence horizontally distributed among diverse bacterial and eucaryotic microbes."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
26,
4763,
1938,
128,
246
] | 5 | [] | [] | 0 | true | Repeat | Bacterial surface protein 26-residue repeat | Bacterial surface protein 26-residue repeat | Liste_lipo_26 | 8 |
IPR011892 | 11,892 | Cytidylate kinase, archaeal-type | Cyt_kin_arch | Family | 1,202 | false | false | Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by . | [
"GO:0005524",
"GO:0016776",
"GO:0006139"
] | [
"ATP binding",
"phosphotransferase activity, phosphate group as acceptor",
"nucleobase-containing compound metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00239",
"TIGR02173"
] | [
"Cytidyl_kinase_type2",
"cyt_kin_arch"
] | [
1052,
1179
] | 2 | [
"EC",
"METACYC"
] | [
"2.7.4.25",
"PWY-7205"
] | [
"EC:2.7.4.25",
"METACYC:PWY-7205"
] | 2 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Menopon gallinae",
"ecological metagenomes"
] | [
982,
194,
1,
25
] | 4 | [] | [] | 0 | true | Family | Cytidylate kinase, archaeal-type | Cytidylate kinase, archaeal-type | Cyt_kin_arch | 7 |
IPR011893 | 11,893 | Selenoprotein, Rdx-type | Selenoprotein_Rdx-typ | Family | 11,876 | false | false | This entry represents the Rdx family of selenoproteins, which includes mammalian selenoproteins SelW, SelV, SelT and SelH, bacterial SelW-like proteins and cysteine-containing proteins of unknown function in all three domains of life. Mammalian Rdx12 and its fish selenoprotein orthologues are also members of this famil... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF10262",
"TIGR02174"
] | [
"Rdx",
"CXXU_selWTH"
] | [
11549,
10819
] | 2 | [] | [] | [] | 0 | [
"2fa8",
"2ljk",
"2npb",
"2obk",
"2ojl",
"2oka",
"2p0g",
"3dex"
] | 8 | [
"PUB00010227",
"PUB00044486",
"PUB00044487",
"PUB00053376",
"PUB00053377",
"PUB00053378",
"PUB00053379",
"PUB00053380"
] | [
"12405536",
"11278576",
"17034973",
"17503775",
"19466610",
"19747065",
"18198219",
"19766117"
] | [
"Selenoprotein W gene regulation by selenium in L8 cells.",
"Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells.",
"Identification of novel genes expressed in hypoxic brain condition by fluorescence differential display."... | [
2002,
2001,
2007,
2007,
2009,
2009,
2008,
2009
] | 8 | [] | [
"IPR019389"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
297,
4618,
6884,
77
] | 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",
"Zea mays"
] | [
14,
2,
8,
5,
10,
9,
1,
6,
12,
4
] | 10 | true | Family | Selenoprotein, Rdx-type | Selenoprotein, Rdx-type | Selenoprotein_Rdx-typ | 5 |
IPR011894 | 11,894 | 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate | PorC_KorC | Domain | 3,887 | false | false | A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins (Helicobacter pylori (Campylobacter pylori)) used as the acceptor. Several related four-subunit enzymes may exist in the same sp... | [
"GO:0016625"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02175"
] | [
"PorC_KorC"
] | [
3887
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.2.7",
"1.2.7.1",
"PWY-5392",
"PWY-5483",
"PWY-5493",
"PWY-5497",
"PWY-5538",
"PWY-5600",
"PWY-6142",
"PWY-6583",
"PWY-6587",
"PWY-6588",
"PWY-6863",
"PWY-6876",
"PWY-8189",
"PWY-8275",
"PWY-8303",
"PWY-8377"
] | [
"EC:1.2.7",
"EC:1.2.7.1",
"METACYC:PWY-5392",
"METACYC:PWY-5483",
"METACYC:PWY-5493",
"METACYC:PWY-5497",
"METACYC:PWY-5538",
"METACYC:PWY-5600",
"METACYC:PWY-6142",
"METACYC:PWY-6583",
"METACYC:PWY-6587",
"METACYC:PWY-6588",
"METACYC:PWY-6863",
"METACYC:PWY-6876",
"METACYC:PWY-8189",
... | 18 | [
"2raa",
"9bt4"
] | 2 | [
"PUB00002295"
] | [
"8550425"
] | [
"Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima."
] | [
1996
] | 1 | [
"IPR019752"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
834,
2884,
169
] | 3 | [] | [] | 0 | true | Domain | 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate | 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate | PorC_KorC | 7 |
IPR011896 | 11,896 | 2-oxoacid:acceptor oxidoreductase, beta subunit | OFOB | Family | 3,457 | false | false | A number of anaerobic and microaerophilic bacterial species lack pyruvate dehydrogenase and have instead a much smaller enzyme complex consisting of a 2-oxoacid oxidoreductase with either ferredoxin or flavodoxin used as the acceptor. 2-oxoacid oxidoreductases are also found in the Archaea. The enzyme complex can compr... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02177"
] | [
"PorB_KorB"
] | [
3457
] | 1 | [
"EC",
"GP",
"GP"
] | [
"1.2.7.11",
"GenProp0839",
"GenProp0842"
] | [
"EC:1.2.7.11",
"GP:GenProp0839",
"GP:GenProp0842"
] | 3 | [
"5b46",
"5b47",
"5b48",
"6n2n",
"6n2o"
] | 5 | [
"PUB00002295",
"PUB00074309",
"PUB00074310",
"PUB00074311",
"PUB00090990"
] | [
"8550425",
"6266826",
"6266827",
"1555599",
"16466637"
] | [
"Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima.",
"Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium.",
"The catal... | [
1996,
1981,
1981,
1992,
2006
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Geodia barretti",
"unclassified sequences"
] | [
1141,
2234,
5,
77
] | 4 | [] | [] | 0 | true | Family | 2-oxoacid:acceptor oxidoreductase, beta subunit | 2-oxoacid:acceptor oxidoreductase, beta subunit | OFOB | 9 |
IPR011897 | 11,897 | Translation elongation factor P-like, YeiP | Transl_elong_p-like_YeiP | Family | 2,336 | false | false | This entry represents homologues of the translation factors elongation factor P ( ), which play a role in translation of XP(P)X-containing proteins and are involved in the detection of the cell's metabolic state via lysine acylation [ ]. Members of this family are found mainly in gammaproteobacteria, including Escheric... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM",
"NCBIFAM"
] | [
"MF_00646",
"NF003392",
"TIGR02178"
] | [
"EFP",
"PRK04542.1",
"yeiP"
] | [
2286,
2328,
1802
] | 3 | [] | [] | [] | 0 | [
"8s8u"
] | 1 | [
"PUB00162637"
] | [
"39622818"
] | [
"EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences."
] | [
2024
] | 1 | [
"IPR020599"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
2298,
3,
35
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Translation elongation factor P-like, YeiP | Translation elongation factor P-like, YeiP | Transl_elong_p-like_YeiP | 9 |
IPR011898 | 11,898 | 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate | PorD_KorD | Family | 2,001 | false | false | A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This entry describes the delta subunit... | [
"GO:0016625",
"GO:0051539"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor",
"4 iron, 4 sulfur cluster binding"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02179"
] | [
"PorD_KorD"
] | [
2001
] | 1 | [] | [] | [] | 0 | [
"5c4i",
"5exd",
"5exe",
"9bt4"
] | 4 | [] | [] | [] | [] | 0 | [] | [
"IPR053389",
"IPR054812"
] | 0 | 2 | 0 | [
"Archaea",
"Bacteria",
"metagenomes"
] | [
767,
1140,
94
] | 3 | [] | [] | 0 | true | Family | 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate | 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate | PorD_KorD | 8 |
IPR011899 | 11,899 | Glutaredoxin, eukaryotic/virial | Glutaredoxin_euk/vir | Domain | 9,129 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02180"
] | [
"GRX_euk"
] | [
9129
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"R-HSA-499943",
"R-MMU-499943",
"R-RNO-499943",
"R-SSC-499943"
] | [
"REACTOME:R-HSA-499943",
"REACTOME:R-MMU-499943",
"REACTOME:R-RNO-499943",
"REACTOME:R-SSC-499943"
] | 4 | [
"1b4q",
"1jhb",
"1kte",
"1z7p",
"1z7r",
"2cq9",
"2e7p",
"2fls",
"2ht9",
"2hze",
"2hzf",
"2jac",
"2jad",
"2lv3",
"2v6o",
"2x8c",
"2x8g",
"2x8h",
"2x99",
"3c1r",
"3c1s",
"3ctf",
"3ctg",
"3d4m",
"3d5j",
"3fz9",
"3fza",
"3h4k",
"3h8q",
"3l4n",
"3rhb",
"3rhc"... | 117 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2004,
1998,
1999,
2005,
2005
] | 10 | [
"IPR014025"
] | [] | 1 | 0 | 1 | [
"Candidatus Arcanibacter lacustris",
"Chordopoxvirinae",
"Eukaryota"
] | [
1,
46,
9082
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
18,
2,
6,
2,
6,
11,
2,
8,
5,
4,
3,
13
] | 12 | true | Domain | Glutaredoxin, eukaryotic/virial | Glutaredoxin, eukaryotic/virial | Glutaredoxin_euk/vir | 2 |
IPR011900 | 11,900 | Glutaredoxin, GrxC | GRX_bact | Family | 8,709 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [
"GO:0045454"
] | [
"cell redox homeostasis"
] | [
"biological_process"
] | 1 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02181",
"cd03418"
] | [
"GRX_bact",
"GRX_GRXb_1_3_like"
] | [
8586,
8555
] | 2 | [] | [] | [] | 0 | [
"1fov",
"2khp",
"2klx",
"2mzc",
"3grx",
"3lgc",
"3msz",
"3qmx",
"4mja",
"4mjb",
"4mjc",
"4mje",
"4tr0",
"4tr1"
] | 14 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015498",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00032967",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"7937896",
"14962389",
"9860827",
"10493864",
"9973569",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
1994,
2004,
1998,
1999,
1999,
2005,
2005
] | 12 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"metagenomes"
] | [
8496,
24,
93,
96
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glutaredoxin, GrxC | Glutaredoxin, GrxC | GRX_bact | 6 |
IPR011901 | 11,901 | Glutaredoxin-2 | Grx2 | Family | 1,789 | false | false | This family includes the highly abundant Escherichia coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC [ ]. Unlike the other two E. coli glutaredoxins, Grx2 appears to be unable to reduce ribonucleotide reductase [ ], and may have more to do with resistance to redox stress [ ]. Purified Grx... | [
"GO:0005829"
] | [
"cytosol"
] | [
"cellular_component"
] | 1 | [
"SFLD",
"NCBIFAM"
] | [
"SFLDG01204",
"TIGR02182"
] | [
"Grx2-like.1",
"GRXB"
] | [
1279,
1787
] | 2 | [] | [] | [] | 0 | [
"1g7o",
"3ir4",
"4ksm",
"4kx4",
"7d9l",
"7dkp",
"7dkr"
] | 7 | [
"PUB00015499",
"PUB00015500",
"PUB00080848",
"PUB00081920"
] | [
"15123823",
"11741965",
"9111025",
"25004967"
] | [
"Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.",
"Characterization of Escherichia coli null mutants for glutaredoxin 2.",
"Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli.... | [
2004,
2002,
1997,
2014
] | 4 | [
"IPR040079"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"organismal metagenomes"
] | [
1676,
110,
3
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glutaredoxin-2 | Glutaredoxin-2 | Grx2 | 7 |
IPR011902 | 11,902 | Glutaredoxin, GrxA | GRXA | Family | 1,903 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [
"GO:0009055",
"GO:0015035",
"GO:0045454"
] | [
"electron transfer activity",
"protein-disulfide reductase activity",
"cell redox homeostasis"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02183"
] | [
"GRXA"
] | [
1903
] | 1 | [] | [] | [] | 0 | [
"1ego",
"1egr",
"1grx",
"1qfn"
] | 4 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015499",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"15123823",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2004,
2004,
1998,
1999,
2005,
2005
] | 11 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified sequences"
] | [
1897,
6
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glutaredoxin, GrxA | Glutaredoxin, GrxA | GRXA | 6 |
IPR011903 | 11,903 | Disulfide oxidoreductase TON_0319-like | TON_0319-like | Family | 525 | false | false | This group of proteins found in bacteria and archaea contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. Many members of this family are selenoproteins. Member protein TON_0319 from Thermococcus onnurineus ( ) was shown modulate the redox state of the CxxC disul... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02187"
] | [
"PDO_seleno_TRX"
] | [
525
] | 1 | [] | [] | [] | 0 | [
"1a8l",
"1j08",
"2ayt",
"2hls",
"2ywm"
] | 5 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927",
"PUB00159278"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611",
"28251348"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2004,
1998,
1999,
2005,
2005,
2017
] | 11 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
213,
294,
18
] | 3 | [] | [] | 0 | true | Family | Disulfide oxidoreductase TON_0319-like | Disulfide oxidoreductase TON_0319-like | TON_0319-like | 9 |
IPR011904 | 11,904 | Acetate-CoA ligase | Ac_CoA_lig | Family | 26,589 | false | false | Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme) is a ubiquitous enzyme, found in both prokaryotes and eukaryotes, which catalyses the formation of acetyl-CoA from acetate, coenzyme A (CoA) and ATP as shown below [ ]: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA The activity... | [
"GO:0003987",
"GO:0016208",
"GO:0019427"
] | [
"acetate-CoA ligase activity",
"AMP binding",
"acetyl-CoA biosynthetic process from acetate"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01123",
"TIGR02188"
] | [
"Ac_CoA_synth",
"Ac_CoA_lig_AcsA"
] | [
15563,
26568
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"6.2.1.1",
"GenProp0480",
"GenProp1379",
"GenProp1437",
"GenProp1687",
"GenProp1715",
"GenProp1722",
"GenProp1749",
"PWY-5108",
"PWY-5132",
"PWY-5133",
"PWY-6672",
"PWY-7118",
"PWY-7857",
"PWY-8303",
"PWY-8328",
"R-DDI-2151201",
"R-DDI-71384",
"R-DME-71384",
"R-HSA-2151201",
... | [
"EC:6.2.1.1",
"GP:GenProp0480",
"GP:GenProp1379",
"GP:GenProp1437",
"GP:GenProp1687",
"GP:GenProp1715",
"GP:GenProp1722",
"GP:GenProp1749",
"METACYC:PWY-5108",
"METACYC:PWY-5132",
"METACYC:PWY-5133",
"METACYC:PWY-6672",
"METACYC:PWY-7118",
"METACYC:PWY-7857",
"METACYC:PWY-8303",
"METAC... | 26 | [
"1pg3",
"1pg4",
"1ry2",
"2p20",
"2p2b",
"2p2f",
"2p2j",
"2p2m",
"2p2q",
"5ifi",
"5jrh",
"5k85",
"5k8f",
"5u29",
"5vpv",
"7kcp",
"7kdn",
"7kds",
"7kno",
"7knp",
"7kq6",
"7kqz",
"7kvy",
"7l3p",
"7l3q",
"7l4g",
"7mmz",
"8eps",
"8g0r",
"8g0s",
"8g0t",
"8g0u"... | 55 | [
"PUB00028098",
"PUB00028099",
"PUB00028100"
] | [
"15316652",
"14769018",
"12627952"
] | [
"Acetyl-coenzyme A synthetase (AMP forming).",
"Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP.",
"The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-5'-propylphosphate and coenzyme A."
] | [
2004,
2004,
2003
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1121,
18887,
6209,
372
] | 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,
2,
4,
2,
1,
7,
4,
1,
5,
2,
2,
1,
4
] | 13 | true | Family | Acetate-CoA ligase | Acetate-CoA ligase | Ac_CoA_lig | 7 |
IPR011905 | 11,905 | Glutaredoxin-like, plant II | GlrX-like_pln_2 | Family | 9,391 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [] | [] | [] | 0 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR10168",
"TIGR02189"
] | [
"",
"GlrX-like_plant"
] | [
9326,
8690
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2004,
1998,
1999,
2005,
2005
] | 10 | [] | [] | 0 | 0 | null | [
"Embryophyta"
] | [
9391
] | 1 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
57,
22,
47
] | 3 | true | Family | Glutaredoxin-like, plant II | Glutaredoxin-like, plant II | GlrX-like_pln_2 | 6 |
IPR011906 | 11,906 | Glutaredoxin domain | Glutaredoxin_dom | Domain | 1,534 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02190"
] | [
"GlrX-dom"
] | [
1534
] | 1 | [] | [] | [] | 0 | [
"1nm3"
] | 1 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2004,
1998,
1999,
2005,
2005
] | 10 | [
"IPR014025"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
1514,
7,
13
] | 3 | [] | [] | 0 | true | Domain | Glutaredoxin domain | Glutaredoxin domain | Glutaredoxin_dom | 6 |
IPR011907 | 11,907 | Ribonuclease III | RNase_III | Family | 28,207 | false | false | This family consists of ribonuclease III (RNase III). This ubiquitous enzyme specifically cleaves double-stranded rRNA and is found in all bacteria and eukaryotes [ ]. In bacteria its main role is the processing of pre-rRNAs, where the large precursor ribosomal RNA molecules are cleaved at specific sites to produce the... | [
"GO:0003723",
"GO:0004525",
"GO:0006364"
] | [
"RNA binding",
"ribonuclease III activity",
"rRNA processing"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00104",
"TIGR02191"
] | [
"RNase_III",
"RNaseIII"
] | [
28103,
25099
] | 2 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.26.3",
"R-CEL-203927",
"R-CEL-426486",
"R-HSA-203927",
"R-MMU-203927",
"R-MMU-426486"
] | [
"EC:3.1.26.3",
"REACTOME:R-CEL-203927",
"REACTOME:R-CEL-426486",
"REACTOME:R-HSA-203927",
"REACTOME:R-MMU-203927",
"REACTOME:R-MMU-426486"
] | 6 | [
"1o0w",
"1rc7",
"1yyk",
"1yyo",
"1yyw",
"1yz9",
"2a11",
"2ez6",
"2nue",
"2nuf",
"2nug",
"3c4b",
"3c4t",
"3n3w",
"4m2z",
"4m30",
"5b16",
"6lxd",
"6lxe",
"6v5b",
"6v5c",
"7dey",
"7eld",
"7ele",
"7r97",
"7zpi",
"7zpj",
"7zpk",
"9asm",
"9asn",
"9aso",
"9asp"... | 33 | [
"PUB00010737",
"PUB00028101",
"PUB00028102"
] | [
"11738048",
"11809414",
"16155207"
] | [
"Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.",
"Ribonuclease III: new sense from nuisance.",
"Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 A."
] | [
2001,
2002,
2005
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
93,
24696,
2708,
59,
651
] | 5 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Escherichia coli (strain K12)",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus",
"Zea mays"
] | [
8,
2,
1,
2,
1,
1,
13,
4,
19
] | 9 | true | Family | Ribonuclease III | Ribonuclease III | RNase_III | 3 |
IPR011908 | 11,908 | Lipopolysaccharide heptosyltransferase I | LipoPS_heptosylTferase-I | Family | 5,150 | false | false | This family consists of examples of ADP-heptose:LPS heptosyltransferase I, an enzyme of LPS inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria [ ]. | [
"GO:0008920",
"GO:0009244"
] | [
"lipopolysaccharide heptosyltransferase activity",
"lipopolysaccharide core region biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02193"
] | [
"heptsyl_trn_I"
] | [
5150
] | 1 | [
"EC",
"GP",
"GP",
"GP"
] | [
"2.4.99.23",
"GenProp0203",
"GenProp1647",
"GenProp1651"
] | [
"EC:2.4.99.23",
"GP:GenProp0203",
"GP:GenProp1647",
"GP:GenProp1651"
] | 4 | [
"2gt1",
"2h1f",
"2h1h",
"6dfe"
] | 4 | [
"PUB00015501"
] | [
"9831648"
] | [
"Cloning, sequencing, and characterization of the lipopolysaccharide biosynthetic enzyme heptosyltransferase I gene (waaC) from Campylobacter jejuni and Campylobacter coli."
] | [
1998
] | 1 | [
"IPR002201"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Nitrosopumilus salarius BD31",
"Eukaryota",
"metagenomes"
] | [
5084,
1,
4,
61
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Lipopolysaccharide heptosyltransferase I | Lipopolysaccharide heptosyltransferase I | LipoPS_heptosylTferase-I | 7 |
IPR011909 | 11,909 | Glutaredoxin-like protein NrdH | GlrX_NrdH | Family | 4,820 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [
"GO:0045454"
] | [
"cell redox homeostasis"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02194"
] | [
"GlrX_NrdH"
] | [
4820
] | 1 | [
"GP"
] | [
"GenProp0289"
] | [
"GP:GenProp0289"
] | 1 | [
"1h75",
"1r7h",
"4f2i",
"4fiw",
"4hs1",
"4k8m"
] | 6 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015502",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"11441020",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2001,
2004,
1998,
1999,
2005,
2005
] | 11 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Caudoviricetes",
"Opisthokonta",
"ecological metagenomes"
] | [
4797,
8,
2,
13
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glutaredoxin-like protein NrdH | Glutaredoxin-like protein NrdH | GlrX_NrdH | 1 |
IPR011910 | 11,910 | ADP-heptose--LPS heptosyltransferase 2 | RfaF | Family | 6,017 | false | false | This family consists of ADP-heptose--LPS heptosyltransferase 2, an enzyme of the lipopolysaccharide (LPS) inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria [ , ]. | [
"GO:0016757",
"GO:0009103"
] | [
"glycosyltransferase activity",
"lipopolysaccharide biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02195"
] | [
"heptsyl_trn_II"
] | [
6017
] | 1 | [
"EC",
"GP",
"GP"
] | [
"2.4.99.24",
"GenProp0203",
"GenProp1651"
] | [
"EC:2.4.99.24",
"GP:GenProp0203",
"GP:GenProp1651"
] | 3 | [
"1psw"
] | 1 | [
"PUB00084342",
"PUB00084343"
] | [
"9119477",
"9266718"
] | [
"Identification of the ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD) and heptosyltransferase II (rfaF) biosynthesis genes from nontypeable Haemophilus influenzae 2019.",
"Deletion of the heptosyltransferase genes rfaC and rfaF in Escherichia coli K-12 results in an Re-type lipopolysaccharide with a high degree... | [
1997,
1997
] | 2 | [
"IPR002201"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4,
5903,
7,
103
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | ADP-heptose--LPS heptosyltransferase 2 | ADP-heptose--LPS heptosyltransferase 2 | RfaF | 8 |
IPR011911 | 11,911 | Glutaredoxin-like protein, YruB | GlrX_YruB | Family | 1,168 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02196"
] | [
"GlrX_YruB"
] | [
1168
] | 1 | [] | [] | [] | 0 | [
"3zij",
"3zit"
] | 2 | [
"PUB00000510",
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927",
"PUB00106672"
] | [
"1637309",
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611",
"23936007"
] | [
"Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum.",
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",... | [
1992,
1988,
1988,
1989,
1991,
2004,
2004,
1998,
1999,
2005,
2005,
2013
] | 12 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Fromanvirus",
"ecological metagenomes"
] | [
18,
1127,
3,
20
] | 4 | [] | [] | 0 | true | Family | Glutaredoxin-like protein, YruB | Glutaredoxin-like protein, YruB | GlrX_YruB | 9 |
IPR011912 | 11,912 | ADP-L-glycero-D-manno-heptose-6-epimerase | Heptose_epim | Family | 6,035 | false | false | Lipopolysaccharides (LPS) are glycolipids that consitutes the outer monolayer of the outer membranes of most Gram-negative bacteria [ ]. They consist of lipid A (endotoxin) which anchors LPS to the outer membrane, a non-repeating core oligosachharide, and an immunogenic O-antigen repeat polymer, which is an oligosaccha... | [
"GO:0008712",
"GO:0050661",
"GO:0005975"
] | [
"ADP-glyceromanno-heptose 6-epimerase activity",
"NADP binding",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_01601",
"TIGR02197",
"cd05248"
] | [
"Heptose_epimerase",
"heptose_epim",
"ADP_GME_SDR_e"
] | [
5249,
6030,
5077
] | 3 | [
"EC",
"GP",
"GP"
] | [
"5.1.3.20",
"GenProp0203",
"GenProp1239"
] | [
"EC:5.1.3.20",
"GP:GenProp0203",
"GP:GenProp1239"
] | 3 | [
"1eq2",
"2x6t",
"2x86",
"3sxp",
"4ej0"
] | 5 | [
"PUB00000419",
"PUB00024627",
"PUB00027779",
"PUB00027780",
"PUB00028103",
"PUB00081093",
"PUB00081094",
"PUB00081095",
"PUB00081096",
"PUB00081097",
"PUB00081102"
] | [
"7742302",
"10896473",
"12604213",
"12604210",
"12045108",
"19011750",
"19011748",
"20423462",
"19027726",
"19061874",
"10089470"
] | [
"Short-chain dehydrogenases/reductases (SDR).",
"The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist.",
"Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs).",
"Short-chain dehydrogenases/reductases (SDR): the 2002 update.",
"Lipopolysa... | [
1995,
2000,
2003,
2003,
2002,
2008,
2008,
2010,
2009,
2009,
1999
] | 11 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanococcales",
"metagenomes"
] | [
5886,
50,
11,
88
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | ADP-L-glycero-D-manno-heptose-6-epimerase | ADP-L-glycero-D-manno-heptose-6-epimerase | Heptose_epim | 8 |
IPR011913 | 11,913 | RfaE bifunctional protein, domain I | RfaE_dom_I | Domain | 8,975 | false | false | RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in some other genome. The longer, N-terminal domain I (this family) is suggested to act in D-glycero-D-manno-heptose 1-p... | [
"GO:0016773",
"GO:0016779",
"GO:0005975"
] | [
"phosphotransferase activity, alcohol group as acceptor",
"nucleotidyltransferase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM",
"CDD"
] | [
"TIGR02198",
"cd01172"
] | [
"rfaE_dom_I",
"RfaE_like"
] | [
7340,
8966
] | 2 | [
"EC",
"EC",
"GP",
"GP"
] | [
"2.7.1.167",
"2.7.7.70",
"GenProp0203",
"GenProp1239"
] | [
"EC:2.7.1.167",
"EC:2.7.7.70",
"GP:GenProp0203",
"GP:GenProp1239"
] | 4 | [
"4e84",
"4e8w",
"4e8y",
"4e8z"
] | 4 | [
"PUB00015503"
] | [
"10629197"
] | [
"The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose."
] | [
2000
] | 1 | [
"IPR011611"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
17,
8755,
43,
160
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | RfaE bifunctional protein, domain I | RfaE bifunctional protein, domain I | RfaE_dom_I | 2 |
IPR011914 | 11,914 | RfaE bifunctional protein, domain II | RfaE_dom_II | Domain | 9,055 | false | false | RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in some other genome. Domain I ( ) is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while doma... | [
"GO:0016773",
"GO:0016779",
"GO:0005975"
] | [
"phosphotransferase activity, alcohol group as acceptor",
"nucleotidyltransferase activity",
"carbohydrate metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02199"
] | [
"rfaE_dom_II"
] | [
9055
] | 1 | [
"EC",
"EC",
"GP",
"GP"
] | [
"2.7.1.167",
"2.7.7.70",
"GenProp0203",
"GenProp1239"
] | [
"EC:2.7.1.167",
"EC:2.7.7.70",
"GP:GenProp0203",
"GP:GenProp1239"
] | 4 | [
"5x9q",
"5xf2"
] | 2 | [
"PUB00015503"
] | [
"10629197"
] | [
"The rfaE gene from Escherichia coli encodes a bifunctional protein involved in biosynthesis of the lipopolysaccharide core precursor ADP-L-glycero-D-manno-heptose."
] | [
2000
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
16,
8878,
37,
124
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | RfaE bifunctional protein, domain II | RfaE bifunctional protein, domain II | RfaE_dom_II | 1 |
IPR011915 | 11,915 | Glutaredoxin-like protein, actinobacteria | GlrX_actino | Family | 3,210 | false | false | Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02200"
] | [
"GlrX_actino"
] | [
3210
] | 1 | [] | [] | [] | 0 | [
"2lqo",
"2lqq"
] | 2 | [
"PUB00000560",
"PUB00001738",
"PUB00002504",
"PUB00005575",
"PUB00014033",
"PUB00015562",
"PUB00023503",
"PUB00030238",
"PUB00080925",
"PUB00080927"
] | [
"3286320",
"3152490",
"2668278",
"1994586",
"14713336",
"14962389",
"9860827",
"10493864",
"15706083",
"15814611"
] | [
"Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"Thioredoxin and related proteins in procaryotes.",
"Thioredoxin and glutaredoxin systems.",
"Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"Glutaredoxins: glutathione-dependent r... | [
1988,
1988,
1989,
1991,
2004,
2004,
1998,
1999,
2005,
2005
] | 10 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3139,
2,
69
] | 3 | [] | [] | 0 | true | Family | Glutaredoxin-like protein, actinobacteria | Glutaredoxin-like protein, actinobacteria | GlrX_actino | 9 |
IPR011916 | 11,916 | Lipopolysaccharide heptosyltransferase III, putative | LipoPS_heptosylTferase-III | Family | 1,884 | false | false | This family consists of examples of the putative ADP-heptose:LPS heptosyltransferase III, an enzyme of the lipopolysaccharide (LPS) inner core region biosynthesis. LPS, composed of lipid A, a core region, and O antigen, is found in the outer membrane of Gram-negative bacteria. This enzyme may be less widely distributed... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02201"
] | [
"heptsyl_trn_III"
] | [
1884
] | 1 | [
"GP",
"GP"
] | [
"GenProp0203",
"GenProp1651"
] | [
"GP:GenProp0203",
"GP:GenProp1651"
] | 2 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR002201"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"ecological metagenomes"
] | [
1873,
2,
9
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Lipopolysaccharide heptosyltransferase III, putative | Lipopolysaccharide heptosyltransferase III, putative | LipoPS_heptosylTferase-III | 6 |
IPR011917 | 11,917 | ABC transporter, lipid A-core flippase, MsbA | ABC_transpr_lipidA | Family | 6,684 | 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... | [
"GO:0005524",
"GO:0034040",
"GO:0016020"
] | [
"ATP binding",
"ATPase-coupled lipid transmembrane transporter activity",
"membrane"
] | [
"molecular_function",
"molecular_function",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02203"
] | [
"MsbA_lipidA"
] | [
6684
] | 1 | [
"EC",
"GP",
"PROSITEDOC"
] | [
"7.5.2.6",
"GenProp0204",
"PDOC51237"
] | [
"EC:7.5.2.6",
"GP:GenProp0204",
"PROSITEDOC:PDOC51237"
] | 3 | [
"3b5w",
"3b5x",
"3b5y",
"3b5z",
"3b60",
"5ttp",
"5tv4",
"6bl6",
"6bpl",
"6bpp",
"6o30",
"6uz2",
"6uzl",
"7bcw",
"7met",
"7mew",
"7ph2",
"7ph3",
"7ph4",
"7ph7",
"7rit",
"7sel",
"8dmm",
"8dmo",
"8gk7",
"8tso",
"8tsp",
"8tsq",
"8tsr",
"8tss",
"9bd6",
"9bd7"... | 53 | [
"PUB00004290",
"PUB00014769",
"PUB00015504",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654",
"PUB00050522",
"PUB00060963",
"PUB00095625",
"PUB00095626"
] | [
"9872322",
"9873074",
"12119303",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270",
"18024585",
"19053284",
"28869968",
"19132955"
] | [
"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.",
"ATPase activity of the MsbA lipid flippase of Escherichia coli.",
"ABC transporters: physiology, structur... | [
1998,
1999,
2002,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
2001,
2007,
2008,
2017,
2009
] | 16 | [
"IPR039421"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
6600,
8,
76
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | ABC transporter, lipid A-core flippase, MsbA | ABC transporter, lipid A-core flippase, MsbA | ABC_transpr_lipidA | 2 |
IPR011918 | 11,918 | ABC transporter, ATP-binding/permease protein | ABC_MsbA_ATP-bd | Family | 4,685 | false | false | This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02204"
] | [
"MsbA_rel"
] | [
4685
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015505"
] | [
"12859648"
] | [
"Isolation and characterization of a transposon mutant of Pseudomonas aeruginosa affecting uptake of dibenzothiophene in n-tetradecane."
] | [
2003
] | 1 | [
"IPR039421"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Pezizomycotina",
"ecological metagenomes"
] | [
4660,
2,
23
] | 3 | [] | [] | 0 | true | Family | ABC transporter, ATP-binding/permease protein | ABC transporter, ATP-binding/permease protein | ABC_MsbA_ATP-bd | 1 |
IPR011919 | 11,919 | Cell division protein ZipA | Cell_div_ZipA | Family | 5,560 | false | false | Cell division in bacteria is a complex process driven by the septal ring, a membrane-associated cytoskeletal element that directs the formation of the septum [ ]. Central to formation of the septal ring, and hence cell division itself, is the tubulin-like GTPase protein FtsZ which is the first cell division component t... | [
"GO:0090529",
"GO:0016020"
] | [
"cell septum assembly",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_00509",
"PTHR38685",
"TIGR02205"
] | [
"ZipA",
"",
"septum_zipA"
] | [
4496,
5559,
4513
] | 3 | [] | [] | [] | 0 | [
"1f46",
"1f47",
"1f7w",
"1f7x",
"1s1j",
"1s1s",
"1y2f",
"1y2g",
"9iue"
] | 9 | [
"PUB00009957",
"PUB00024782",
"PUB00028104"
] | [
"10924108",
"10880432",
"9442879"
] | [
"Solution structure of ZipA, a crucial component of Escherichia coli cell division.",
"The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography.",
"Bacterial cell division."
] | [
2000,
2000,
1997
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5487,
7,
66
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Cell division protein ZipA | Cell division protein ZipA | Cell_div_ZipA | 2 |
IPR011920 | 11,920 | Lipid A biosynthesis lauroyl/palmitoleoyl acyltransferase | Lipid_A_LpxL_LpxP | Family | 6,224 | false | false | Bacterial lipopolysachharides (LPS) are glycolipids that make up the outer monolayer of the outer membranes of most Gram-negative bacteria. Though LPS moleculesare variable, they all show the same general features: an outer polysaccharide which is attached to the lipid component, termed lipid A [ ]. The polysaccharide ... | [
"GO:0016740",
"GO:0009245",
"GO:0016020"
] | [
"transferase activity",
"lipid A biosynthetic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01942",
"TIGR02207"
] | [
"Lipid_A_LpxL_LpxP",
"lipid_A_htrB"
] | [
6055,
5947
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.3.1.241",
"GenProp0204",
"GenProp1325",
"GenProp1397",
"GenProp1647",
"PWY-8075",
"PWY-8247",
"PWY-8285",
"PWY-8378"
] | [
"EC:2.3.1.241",
"GP:GenProp0204",
"GP:GenProp1325",
"GP:GenProp1397",
"GP:GenProp1647",
"METACYC:PWY-8075",
"METACYC:PWY-8247",
"METACYC:PWY-8285",
"METACYC:PWY-8378"
] | 9 | [] | 0 | [
"PUB00015506",
"PUB00028103",
"PUB00033945",
"PUB00033946"
] | [
"11830594",
"12045108",
"9791168",
"8894399"
] | [
"An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C.",
"Lipopolysaccharide endotoxins.",
"Molecular basis for structural diversity in the core regions of the lipopolysacchar... | [
2002,
2002,
1998,
1996
] | 4 | [
"IPR004960"
] | [
"IPR030857"
] | 1 | 1 | 0 | [
"Bacteria",
"Opisthokonta",
"metagenomes"
] | [
6181,
8,
35
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Lipid A biosynthesis lauroyl/palmitoleoyl acyltransferase | Lipid A biosynthesis lauroyl/palmitoleoyl acyltransferase | Lipid_A_LpxL_LpxP | 6 |
IPR011921 | 11,921 | Lipid A biosynthesis myristoyltransferase | Lipid_A_MsbB | Family | 2,284 | false | false | Bacterial lipopolysachharides (LPS) are glycolipids that make up the outer monolayer of the outer membranes of most Gram-negative bacteria. Though LPS moleculesare variable, they all show the same general features: an outer polysaccharide which is attached to the lipid component, termed lipid A [ ]. The polysaccharide ... | [
"GO:0016747",
"GO:0009103",
"GO:0009276",
"GO:0016020"
] | [
"acyltransferase activity, transferring groups other than amino-acyl groups",
"lipopolysaccharide biosynthetic process",
"Gram-negative-bacterium-type cell wall",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component",
"cellular_component"
] | 4 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01944",
"TIGR02208"
] | [
"Lipid_A_LpxM",
"lipid_A_msbB"
] | [
2227,
2194
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC"
] | [
"2.3.1.243",
"GenProp0204",
"GenProp1325",
"GenProp1397",
"GenProp1647",
"PWY-8285",
"PWY-8378"
] | [
"EC:2.3.1.243",
"GP:GenProp0204",
"GP:GenProp1325",
"GP:GenProp1397",
"GP:GenProp1647",
"METACYC:PWY-8285",
"METACYC:PWY-8378"
] | 7 | [] | 0 | [
"PUB00028103",
"PUB00033945",
"PUB00033946"
] | [
"12045108",
"9791168",
"8894399"
] | [
"Lipopolysaccharide endotoxins.",
"Molecular basis for structural diversity in the core regions of the lipopolysaccharides of Escherichia coli and Salmonella enterica.",
"The lipooligosaccharides of pathogenic gram-negative bacteria."
] | [
2002,
1998,
1996
] | 3 | [
"IPR004960"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta"
] | [
2282,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Lipid A biosynthesis myristoyltransferase | Lipid A biosynthesis myristoyltransferase | Lipid_A_MsbB | 2 |
IPR011922 | 11,922 | Cell division protein FtsL | Cell_div_FtsL | Family | 8,877 | false | false | FtsL is one of the later proteins active in cell division septum formation. FtsL is small, low in complexity, and highly divergent [ , ]. | [
"GO:0051301",
"GO:0016020"
] | [
"cell division",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"PFAM",
"PANTHER",
"NCBIFAM"
] | [
"MF_00910",
"PF04999",
"PTHR37479",
"TIGR02209"
] | [
"FtsL",
"FtsL",
"",
"ftsL_broad"
] | [
8231,
6136,
5549,
8277
] | 4 | [
"GP",
"GP"
] | [
"GenProp1142",
"GenProp1154"
] | [
"GP:GenProp1142",
"GP:GenProp1154"
] | 2 | [
"8bh1",
"8hhf",
"8hhg",
"8hhh",
"8p1u"
] | 5 | [
"PUB00015509",
"PUB00015542"
] | [
"12626683",
"10986263"
] | [
"Cytokinesis in bacteria.",
"Analysis of the essential cell division gene ftsL of Bacillus subtilis by mutagenesis and heterologous complementation."
] | [
2003,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
8764,
11,
102
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Cell division protein FtsL | Cell division protein FtsL | Cell_div_FtsL | 3 |
IPR011923 | 11,923 | Probable peptidoglycan glycosyltransferase RodA/MrdB | RodA/MrdB | Family | 14,383 | false | false | Treponema pallidum RodA and Escherichia coli MrdB are probable peptidoglycan polymerases that are essential for cell wall elongation [ ]. RodA is a member of the FtsW/RodA/SpoVE family. It is found only in species with rod (or spiral) shapes. RodA is required for the maintenance of the rod cell shape and is essential f... | [
"GO:0008360",
"GO:0016020"
] | [
"regulation of cell shape",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_02079",
"TIGR02210"
] | [
"PGT_RodA",
"rodA_shape"
] | [
9832,
14336
] | 2 | [
"EC",
"GP"
] | [
"2.4.99.28",
"GenProp0166"
] | [
"EC:2.4.99.28",
"GP:GenProp0166"
] | 2 | [
"6bar",
"6bas",
"6pl5",
"6pl6",
"8tj3"
] | 5 | [
"PUB00042955",
"PUB00071895",
"PUB00086588"
] | [
"2644207",
"9622350",
"27643381"
] | [
"Nucleotide sequence of the rodA gene, responsible for the rod shape of Escherichia coli: rodA and the pbpA gene, encoding penicillin-binding protein 2, constitute the rodA operon.",
"Control of cell shape and elongation by the rodA gene in Bacillus subtilis.",
"Bacterial cell wall biogenesis is mediated by SED... | [
1989,
1998,
2016
] | 3 | [
"IPR001182"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
14078,
21,
284
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Probable peptidoglycan glycosyltransferase RodA/MrdB | Probable peptidoglycan glycosyltransferase RodA/MrdB | RodA/MrdB | 1 |
IPR011924 | 11,924 | Lipoprotein releasing system, ATP-binding protein | LolD_lipo_ATP-bd | Family | 5,475 | false | false | This entry represents LolD, a member of the ABC transporter family. LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on the residue immediately following the modified N-terminal Cys residue,... | [
"GO:0005524",
"GO:0044873",
"GO:0016020"
] | [
"ATP binding",
"lipoprotein localization to membrane",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02211"
] | [
"LolD_lipo_ex"
] | [
5475
] | 1 | [
"EC",
"GP"
] | [
"7.6.2.-",
"GenProp0207"
] | [
"EC:7.6.2.-",
"GP:GenProp0207"
] | 2 | [
"7arh",
"7ari",
"7arj",
"7ark",
"7arl",
"7arm",
"7mdx",
"7mdy",
"7v8i",
"7v8l",
"7v8m",
"9grc",
"9gvk"
] | 13 | [
"PUB00015507",
"PUB00072505"
] | [
"12823819",
"10783239"
] | [
"A mutation in the membrane subunit of an ABC transporter LolCDE complex causing outer membrane localization of lipoproteins against their inner membrane-specific signals.",
"A new ABC transporter mediating the detachment of lipid-modified proteins from membranes."
] | [
2003,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
5434,
5,
36
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Lipoprotein releasing system, ATP-binding protein | Lipoprotein releasing system, ATP-binding protein | LolD_lipo_ATP-bd | 3 |
IPR011925 | 11,925 | Lipoprotein-releasing system transmembrane protein LolC/E | LolCE_TM | Family | 13,391 | false | false | This entry describes the LolC protein, and its paralog LolE found in some species. These proteins are homologous to permease proteins of ABC transporters. In some species, two paralogs occur, designated LolC and LolE. In others, a single form is found and tends to be designated LolC [ ]. The LolCDE complex releases lip... | [
"GO:0042953",
"GO:0016020"
] | [
"lipoprotein transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02212"
] | [
"lolCE"
] | [
13391
] | 1 | [
"GP"
] | [
"GenProp0207"
] | [
"GP:GenProp0207"
] | 1 | [
"7arh",
"7ari",
"7arj",
"7ark",
"7arl",
"7arm",
"7mdx",
"7mdy",
"7v8i",
"7v8l",
"7v8m",
"9grc",
"9gvk"
] | 13 | [
"PUB00015507",
"PUB00061667",
"PUB00061668"
] | [
"12823819",
"19809197",
"19307584"
] | [
"A mutation in the membrane subunit of an ABC transporter LolCDE complex causing outer membrane localization of lipoproteins against their inner membrane-specific signals.",
"Membrane topology and functional importance of the periplasmic region of ABC transporter LolCDE.",
"Model of mouth-to-mouth transfer of b... | [
2003,
2009,
2009
] | 3 | [] | [
"IPR011926"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
13258,
13,
120
] | 3 | [
"Escherichia coli (strain K12)"
] | [
3
] | 1 | true | Family | Lipoprotein-releasing system transmembrane protein LolC/E | Lipoprotein-releasing system transmembrane protein LolC/E | LolCE_TM | 5 |
IPR011926 | 11,926 | Lipoprotein-releasing system transmembrane protein LolE, gammaproteobacteria type | LolE_gammaproteobact | Family | 1,933 | false | false | This protein is part of an unusual ABC transporter complex that releases lipoproteins from the periplasmic side of the bacterial inner membrane, rather than transport any substrate across the inner membrane. In some species, the permease-like transmembrane protein is represented by two paralogs, LolC and LolE, both in ... | [
"GO:0042953",
"GO:0044874",
"GO:0016020"
] | [
"lipoprotein transport",
"lipoprotein localization to outer membrane",
"membrane"
] | [
"biological_process",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02213"
] | [
"lolE_release"
] | [
1933
] | 1 | [] | [] | [] | 0 | [
"7arh",
"7ari",
"7arj",
"7ark",
"7arl",
"7arm",
"7mdx",
"7mdy",
"7v8i",
"7v8l",
"7v8m",
"9grc",
"9gvk"
] | 13 | [
"PUB00087518"
] | [
"23187171"
] | [
"Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex."
] | [
2013
] | 1 | [
"IPR011925"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota"
] | [
1931,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Lipoprotein-releasing system transmembrane protein LolE, gammaproteobacteria type | Lipoprotein-releasing system transmembrane protein LolE, gammaproteobacteria type | LolE_gammaproteobact | 8 |
IPR011927 | 11,927 | Stage V sporulation protein D | SpoVD_pbp | Family | 1,924 | false | false | This entry describes the SpoVD family of homologues of the cell division protein FtsI, a penicillin binding protein. This family is restricted to Bacillus subtilis and related Gram-positive species with known or suspected endospore formation capability. In these species, the functional equivalent of FtsI is desginated ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02214"
] | [
"spoVD_pbp"
] | [
1924
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR050515"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"metagenomes"
] | [
1917,
7
] | 2 | [] | [] | 0 | true | Family | Stage V sporulation protein D | Stage V sporulation protein D | SpoVD_pbp | 2 |
IPR011928 | 11,928 | Bacteriophage phiJL001, Gp84 | Phage_phiJL001_Gp84 | Family | 2,639 | false | false | This entry describes bacteriophage phiJL001 Gp84 and related proteins in other bacteriophage and prophage regions of bacterial genomes. Homologues are also found in Gene Transfer Agents (GTA) [ ], including ORFg13 (RCAP_rcc01696) of the GTA of Rhodobacter capsulatus (Rhodopseudomonas capsulata) [[see Fig.1, in ]. The f... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02218"
] | [
"phg_TIGR02218"
] | [
2639
] | 1 | [] | [] | [] | 0 | [
"6tba",
"6teh",
"8gtc",
"8rk3",
"8rk6",
"8rk7",
"8vjh"
] | 7 | [
"PUB00055430",
"PUB00055431"
] | [
"11382219",
"12399927"
] | [
"The gene transfer agent of Rhodobacter capsulatus and \"constitutive transduction\" in prokaryotes.",
"Evolutionary implications of phylogenetic analyses of the gene transfer agent (GTA) of Rhodobacter capsulatus."
] | [
2001,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Ecdysozoa",
"Viruses",
"metagenomes"
] | [
2446,
7,
160,
26
] | 4 | [] | [] | 0 | true | Family | Bacteriophage phiJL001, Gp84 | Bacteriophage phiJL001, Gp84 | Phage_phiJL001_Gp84 | 8 |
IPR011929 | 11,929 | NlpC/P60 family, putative phage cell wall peptidase | Phage_pept_NlpC/P60 | Family | 1,708 | false | false | Members of this family show sequence similarity to members of the NlpC/P60 family described by Anantharaman and Aravind [ ]. The NlpC/P60 family includes a number of characterised bacterial cell wall hydrolases. Members of this related family are all found in prophage regions of bacterial genomes. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02219"
] | [
"phage_NlpC_fam"
] | [
1708
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015508"
] | [
"12620121"
] | [
"Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes."
] | [
2003
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Viruses",
"metagenomes"
] | [
1684,
12,
12
] | 3 | [] | [] | 0 | true | Family | NlpC/P60 family, putative phage cell wall peptidase | NlpC/P60 family, putative phage cell wall peptidase | Phage_pept_NlpC/P60 | 8 |
IPR011931 | 11,931 | Tyrosine recombinase XerC | Recomb_XerC | Family | 8,430 | false | false | The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This entry represents XerC, which is closely related to the other chromosomal protein Xe... | [
"GO:0003677",
"GO:0006310",
"GO:0007059",
"GO:0015074",
"GO:0051301"
] | [
"DNA binding",
"DNA recombination",
"chromosome segregation",
"DNA integration",
"cell division"
] | [
"molecular_function",
"biological_process",
"biological_process",
"biological_process",
"biological_process"
] | 5 | [
"NCBIFAM"
] | [
"TIGR02224"
] | [
"recomb_XerC"
] | [
8430
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015510"
] | [
"12823825"
] | [
"Species specificity in the activation of Xer recombination at dif by FtsK."
] | [
2003
] | 1 | [
"IPR023009"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
8357,
4,
69
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Tyrosine recombinase XerC | Tyrosine recombinase XerC | Recomb_XerC | 6 |
IPR011932 | 11,932 | Tyrosine recombinase XerD | Recomb_XerD | Family | 16,974 | false | false | Proteins in this entry are part of the wider so-called "phage" integrase fmaily which describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This entry represents the chr... | [
"GO:0009009",
"GO:0006310"
] | [
"site-specific recombinase activity",
"DNA recombination"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01807",
"TIGR02225"
] | [
"Recomb_XerD",
"recomb_XerD"
] | [
12950,
15648
] | 2 | [] | [] | [] | 0 | [
"1a0p"
] | 1 | [
"PUB00015510",
"PUB00020091"
] | [
"12823825",
"9311978"
] | [
"Species specificity in the activation of Xer recombination at dif by FtsK.",
"Crystal structure of the site-specific recombinase, XerD."
] | [
2003,
1997
] | 2 | [
"IPR023009"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Siphoviridae sp. ctBLh2",
"unclassified sequences"
] | [
16741,
8,
1,
224
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Tyrosine recombinase XerD | Tyrosine recombinase XerD | Recomb_XerD | 5 |
IPR011933 | 11,933 | Double transmembrane domain | Double_TM_dom | Domain | 6,238 | false | false | This entry represents a prokaryotic N-terminal region of about 80 amino acids. The predicted membrane topology by TMHMM puts the N terminus outside and spans the membrane twice, with a cytosolic region of about 25 amino acids between the two transmembrane regions. Member proteins tend to be between 600 and 1000 amino a... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02226"
] | [
"two_anch"
] | [
6238
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR024163"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
168,
5934,
9,
127
] | 4 | [] | [] | 0 | true | Domain | Double transmembrane domain | Double transmembrane domain | Double_TM_dom | 7 |
IPR011935 | 11,935 | Conserved hypothetical protein CHP02231 | CHP02231 | Family | 6,372 | false | false | This family consists of proteins over 500 amino acids long in Caenorhabditis elegans and several bacteria (Pseudomonas aeruginosa, Anabaena sp. (strain PCC 7120), Leptospira interrogans, etc.). The function is unknown. | [] | [] | [] | 0 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR31005",
"TIGR02231"
] | [
"",
""
] | [
6367,
4694
] | 2 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
11,
3664,
2648,
49
] | 4 | [
"Caenorhabditis elegans"
] | [
6
] | 1 | true | Family | Conserved hypothetical protein CHP02231 | Conserved hypothetical protein CHP02231 | CHP02231 | 3 |
IPR011936 | 11,936 | Myxococcus cysteine-rich repeat | Myxo_disulph_rpt | Repeat | 7,328 | false | false | This entry represents a sequence region shared between several proteins of Myxococcus xanthus (strain DK 1622) and some eukaryotic proteins that include human pappalysin-1. The region of about 40 amino acids contains several conserved Cys residues presumed to form disulphide bonds. The region appears in up to 13 repeat... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF13948",
"TIGR02232"
] | [
"DUF4215",
"myxo_disulf_rpt"
] | [
3531,
7223
] | 2 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-381426",
"R-MMU-381426"
] | [
"REACTOME:R-HSA-381426",
"REACTOME:R-MMU-381426"
] | 2 | [
"7ufg",
"7y5n",
"7y5q",
"8a7d",
"8a7e",
"8d8o",
"8hgg",
"8hgh",
"8sl1"
] | 9 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"ecological metagenomes"
] | [
1886,
4,
5429,
9
] | 4 | [
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
16,
8,
6,
13
] | 4 | true | Repeat | Myxococcus cysteine-rich repeat | Myxococcus cysteine-rich repeat | Myxo_disulph_rpt | 9 |
IPR011937 | 11,937 | 2-carboxy-1,4-naphthoquinone phytyltransferase | DHNA_phytyltransferase_MenA | Family | 979 | false | false | This entry represents 2-carboxy-1,4-naphthoquinone phytyltransferase from plants and cyanobacteria. It catalyses the conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylphylloquinone [ ]. | [
"GO:0004659",
"GO:0042372",
"GO:0016020"
] | [
"prenyltransferase activity",
"phylloquinone biosynthetic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01938",
"TIGR02235"
] | [
"MenA_2",
"menA_cyano-plnt"
] | [
920,
958
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00074146"
] | [
"10722690"
] | [
"Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. pcc 6803."
] | [
2000
] | 1 | [
"IPR026046"
] | [] | 1 | 0 | 1 | [
"Cyanobacteriota",
"Eukaryota"
] | [
362,
617
] | 2 | [
"Arabidopsis thaliana",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
3,
4
] | 3 | true | Family | 2-carboxy-1,4-naphthoquinone phytyltransferase | 2-carboxy-1,4-naphthoquinone phytyltransferase | DHNA_phytyltransferase_MenA | 1 |
IPR011938 | 11,938 | DNA recombination/repair protein RadA | DNA_recomb/repair_RadA | Family | 1,017 | false | false | This family consists exclusively of archaeal RadA protein, a homologue of bacterial RecA, eukaryotic RAD51 ( ), and archaeal RadB ( ). This protein is involved in DNA repair and in homologous recombination, it binds and assembles on single-stranded DNA to form a nucleoprotein filament. RadA hydrolyzes ATP in a ssDNA-de... | [
"GO:0003684",
"GO:0005524",
"GO:0008094",
"GO:0006281",
"GO:0006310"
] | [
"damaged DNA binding",
"ATP binding",
"ATP-dependent activity, acting on DNA",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 5 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00348",
"TIGR02236"
] | [
"RadA_arch",
"recomb_radA"
] | [
883,
1005
] | 2 | [] | [] | [] | 0 | [
"1pzn",
"1t4g",
"1xu4",
"2b21",
"2bke",
"2dfl",
"2f1h",
"2f1i",
"2f1j",
"2fpk",
"2fpl",
"2fpm",
"2gdj",
"2i1q",
"2z43",
"2zub",
"2zuc",
"2zud",
"3etl",
"3ew9",
"3ewa",
"3fyh",
"3ntu",
"4a6p",
"4a6x",
"4b2i",
"4b2l",
"4b2p",
"4b32",
"4b33",
"4b34",
"4b35"... | 83 | [
"PUB00015512"
] | [
"11713300"
] | [
"RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination."
] | [
2001
] | 1 | [
"IPR016467"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Candidatus Staskawiczbacteria bacterium RIFCSPHIGHO2_01_FULL_41_41",
"Eukaryota",
"metagenomes"
] | [
933,
1,
44,
39
] | 4 | [] | [] | 0 | true | Family | DNA recombination/repair protein RadA | DNA recombination/repair protein RadA | DNA_recomb/repair_RadA | 8 |
IPR011939 | 11,939 | DNA repair and recombination protein RadB | DNA_repair_and_recomb_RadB | Family | 737 | false | false | The RadB family of archaeal proteins is involved in DNA repair and in homologous recombination [ ]. The proteins contain a conserved triplet of residues (Lys-His-Arg) at their C terminus that is crucial for DNA binding [ ]. RadB does not catalyse strand exchange and does not turn over ATP efficiently. It has been shown... | [
"GO:0003684",
"GO:0005524",
"GO:0006281",
"GO:0006310"
] | [
"damaged DNA binding",
"ATP binding",
"DNA repair",
"DNA recombination"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 4 | [
"HAMAP",
"PIRSF",
"NCBIFAM"
] | [
"MF_00350",
"PIRSF003336",
"TIGR02237"
] | [
"RadB",
"RadB",
"recomb_radB"
] | [
618,
724,
624
] | 3 | [] | [] | [] | 0 | [
"1n0w",
"2cvf",
"2cvh",
"4a6p",
"4a6x",
"4b2i",
"4b2l",
"4b2p",
"4b32",
"4b33",
"4b34",
"4b35",
"4b3b",
"4b3c",
"4b3d",
"4d6p",
"4uqo",
"5fos",
"5fot",
"5fou",
"5fov",
"5fow",
"5fox",
"5fpk",
"5j4h",
"5j4k",
"5j4l",
"5jec",
"5jed",
"5jee",
"5jfg",
"5kdd"... | 69 | [
"PUB00015513",
"PUB00066218"
] | [
"10903318",
"16516228"
] | [
"Both RadA and RadB are involved in homologous recombination in Pyrococcus furiosus.",
"Interactions of RadB, a DNA repair protein in archaea, with DNA and ATP."
] | [
2000,
2006
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Eukaryota",
"Parcubacteria group",
"ecological metagenomes"
] | [
663,
58,
2,
14
] | 4 | [] | [] | 0 | true | Family | DNA repair and recombination protein RadB | DNA repair and recombination protein RadB | DNA_repair_and_recomb_RadB | 7 |
IPR011940 | 11,940 | Meiotic recombination protein Dmc1 | Dmc1 | Family | 2,265 | false | false | Dmc1 is a meiosis-specific RecA homologue [ ]. It is a recombinase required for interhomologue recombination and double-strand break repair during meiosis [ , , , ]. | [
"GO:0000150",
"GO:0003677",
"GO:0007131",
"GO:0005634"
] | [
"DNA strand exchange activity",
"DNA binding",
"reciprocal meiotic recombination",
"nucleus"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"NCBIFAM"
] | [
"TIGR02238"
] | [
"recomb_DMC1"
] | [
2265
] | 1 | [
"REACTOME",
"REACTOME"
] | [
"R-HSA-912446",
"R-MMU-912446"
] | [
"REACTOME:R-HSA-912446",
"REACTOME:R-MMU-912446"
] | 2 | [
"1v5w",
"2zjb",
"4hyy",
"6r3p",
"7c98",
"7c99",
"7c9a",
"7c9c",
"7cgy",
"7ej6",
"7ej7",
"8qqe",
"8r2g",
"9d4n",
"9njr"
] | 15 | [
"PUB00044868",
"PUB00090180",
"PUB00090181",
"PUB00090182"
] | [
"15620352",
"11005857",
"10488231",
"17639081"
] | [
"A protein complex containing Mei5 and Sae3 promotes the assembly of the meiosis-specific RecA homolog Dmc1.",
"Tid1/Rdh54 promotes colocalization of rad51 and dmc1 during meiotic recombination.",
"Random chromosome segregation without meiotic arrest in both male and female meiocytes of a dmc1 mutant of Arabido... | [
2004,
2000,
1999,
2007
] | 4 | [
"IPR016467"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2265
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea mays"
] | [
5,
2,
1,
2,
4,
4,
1,
1,
7
] | 9 | true | Family | Meiotic recombination protein Dmc1 | Meiotic recombination protein Dmc1 | Dmc1 | 3 |
IPR011941 | 11,941 | DNA recombination/repair protein Rad51 | DNA_recomb/repair_Rad51 | Family | 3,792 | false | false | Homologous recombination is an evolutionarily conserved mechanism for the repair of double-strand breaks in DNA and the generation of genetic diversity. The primary function of homologous recombination in mitotic cells is to repair double-strand breaks or single-strand gaps that form as a result of replication fork col... | [
"GO:0000150",
"GO:0003690",
"GO:0003697",
"GO:0008094",
"GO:0000724",
"GO:1990426"
] | [
"DNA strand exchange activity",
"double-stranded DNA binding",
"single-stranded DNA binding",
"ATP-dependent activity, acting on DNA",
"double-strand break repair via homologous recombination",
"mitotic recombination-dependent replication fork processing"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process",
"biological_process"
] | 6 | [
"NCBIFAM"
] | [
"TIGR02239"
] | [
"recomb_RAD51"
] | [
3792
] | 1 | [
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOM... | [
"R-BTA-5685938",
"R-BTA-5685942",
"R-BTA-5693568",
"R-BTA-5693579",
"R-BTA-5693616",
"R-BTA-912446",
"R-CFA-5685938",
"R-CFA-5685942",
"R-CFA-5693568",
"R-CFA-5693579",
"R-CFA-5693616",
"R-CFA-912446",
"R-DME-5693616",
"R-GGA-265976",
"R-GGA-351433",
"R-GGA-5685938",
"R-GGA-5685942",... | [
"REACTOME:R-BTA-5685938",
"REACTOME:R-BTA-5685942",
"REACTOME:R-BTA-5693568",
"REACTOME:R-BTA-5693579",
"REACTOME:R-BTA-5693616",
"REACTOME:R-BTA-912446",
"REACTOME:R-CFA-5685938",
"REACTOME:R-CFA-5685942",
"REACTOME:R-CFA-5693568",
"REACTOME:R-CFA-5693579",
"REACTOME:R-CFA-5693616",
"REACTOME... | 42 | [
"1n0w",
"1szp",
"3lda",
"5h1b",
"5h1c",
"5jzc",
"5np7",
"5nwl",
"7c9a",
"7ejc",
"7eje",
"8bq2",
"8br2",
"8bsc",
"8gyk",
"8jnd",
"8jne",
"8jnf",
"8pbc",
"8pbd",
"8r64",
"8rcd",
"8rcf",
"8uvw",
"8xbt",
"8xbu",
"8xbv",
"8xbw",
"8xbx",
"8xby",
"9b2d",
"9d46"... | 44 | [
"PUB00014057",
"PUB00027524",
"PUB00031260",
"PUB00033348",
"PUB00033349",
"PUB00033350"
] | [
"10390347",
"12442171",
"15235592",
"15568977",
"1581961",
"12778123"
] | [
"The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.",
"Insights into DNA recombination from the structure of a RAD51-BRCA2 complex.",
"Crystal structure of a Rad51 filament.",
"Recombination proteins in yeast.",
"Rad51 protein involved in repa... | [
1999,
2002,
2004,
2004,
1992,
2003
] | 6 | [
"IPR016467"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
3792
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
4,
3,
2,
2,
2,
1,
1,
5,
2,
1,
1,
6
] | 12 | true | Family | DNA recombination/repair protein Rad51 | DNA recombination/repair protein Rad51 | DNA_recomb/repair_Rad51 | 6 |
IPR011942 | 11,942 | Poly(3-hydroxyalkanoate) depolymerase | PHA_depoly_arom | Family | 1,057 | false | false | This family consists of the polyhydroxyalkanoic acid (PHA) depolymerase of Pseudomonas oleovorans and related species. This enzyme is part of polyester storage and mobilisation system as in many bacteria. However, species containing this enzyme are unusual in their capacity to produce aromatic polyesters when grown on ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02240"
] | [
"PHA_depoly_arom"
] | [
1057
] | 1 | [
"GP"
] | [
"GenProp0055"
] | [
"GP:GenProp0055"
] | 1 | [] | 0 | [
"PUB00015514"
] | [
"10506180"
] | [
"Novel biodegradable aromatic plastics from a bacterial source. Genetic and biochemical studies on a route of the phenylacetyl-coa catabolon."
] | [
1999
] | 1 | [
"IPR050471"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Ripduovirus RP12",
"marine sediment metagenome"
] | [
1053,
2,
2
] | 3 | [] | [] | 0 | true | Family | Poly(3-hydroxyalkanoate) depolymerase | Poly(3-hydroxyalkanoate) depolymerase | PHA_depoly_arom | 8 |
IPR011943 | 11,943 | HAD-superfamily hydrolase, subfamily IIID | HAD-SF_hydro_IIID | Domain | 2,341 | false | false | This family of sequences appears to belong to the Haloacid Dehalogenase (HAD) superfamily of enzymes by virtue of the presence of three catalytic domains [ ], in this case: LLVLD(ILV)D(YH)T, I(VMG)IWS, and (DN)(VC)K(PA)Lx{15-17}T(IL)(MH)(FV)DD(IL)(GRS)(RK)N. Since this family has no large "cap" domain [ ] between motif... | [
"GO:0004721",
"GO:0005634"
] | [
"phosphoprotein phosphatase activity",
"nucleus"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02245"
] | [
"HAD_IIID1"
] | [
2341
] | 1 | [
"EC"
] | [
"3.1.3.16"
] | [
"EC:3.1.3.16"
] | 1 | [
"3shq"
] | 1 | [
"PUB00003337",
"PUB00009540",
"PUB00009589"
] | [
"7966317",
"10956028",
"11601995"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and ca... | [
1994,
2000,
2001
] | 3 | [
"IPR004274"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
2341
] | 1 | [
"Arabidopsis thaliana",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Zea mays"
] | [
3,
3,
1,
1,
1,
2,
3,
3
] | 8 | true | Domain | HAD-superfamily hydrolase, subfamily IIID | HAD-superfamily hydrolase, subfamily IIID | HAD-SF_hydro_IIID | 7 |
IPR011944 | 11,944 | Steroid delta5-4-isomerase | Steroid_delta5-4_isomerase | Family | 9,257 | false | false | This entry consists mostly of uncharacterised proteins found in a number of bacterial species, including Streptomyces, Xanthomonas, Oceanobacillus iheyensis, Caulobacter crescentus CB15, and Xylella fastidiosa. One protein in this entry ( from Comamonas testosteroni) has been shown to be a steroid delta-isomerase enzym... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02246"
] | [
""
] | [
9257
] | 1 | [] | [] | [] | 0 | [
"1buq",
"1isk",
"1ocv",
"1ogz",
"1ohp",
"1ohs",
"1qjg",
"3cu3",
"3gzr",
"3h51",
"3m8c",
"3mhe",
"3mki",
"3myt",
"3nbr",
"3nhx",
"3nm2",
"3nuv",
"3nxj",
"3ov4",
"3rob",
"3t8u",
"3unl",
"4i4k",
"4l7k",
"4ovm",
"5dre",
"5ugi",
"8cho",
"8vez",
"8vfq"
] | 31 | [
"PUB00023749",
"PUB00026137",
"PUB00028107",
"PUB00028108"
] | [
"9778345",
"9103200",
"2271654",
"12734184"
] | [
"Solution structure of Delta 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate.",
"Solution structure of 3-oxo-delta5-steroid isomerase.",
"Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction.",
"Origin of the different pH activity ... | [
1998,
1997,
1990,
2003
] | 4 | [] | [
"IPR016887"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
33,
8885,
296,
43
] | 4 | [] | [] | 0 | true | Family | Steroid delta5-4-isomerase | Steroid delta5-4-isomerase | Steroid_delta5-4_isomerase | 4 |
IPR011945 | 11,945 | Predicted HAD-superfamily phosphatase, subfamily IA/Epoxide hydrolase, N-terminal | HAD-SF_ppase_IA/epoxid_hydro_N | Domain | 2,091 | false | false | This entry represents a small clade of sequences from the metazoa and bacteria. In eukaryotes, this domain exists as an N-terminal fusion to the soluble epoxide hydrolase enzyme and has recently been shown to be an active phosphatase, although the nature of the biological substrate is unclear [ ]. These appear to be me... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02247"
] | [
"HAD-1A3-hyp"
] | [
2091
] | 1 | [
"EC",
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"3.1.3.76",
"3.3.2.10",
"PWY-6710",
"PWY-7778",
"PWY-8356",
"PWY-8395",
"PWY-8397",
"PWY-8399",
"PWY-8400",
"R-HSA-2142670",
"R-HSA-77289",
"R-HSA-9018682",
"R-HSA-9033241",
"R-MMU-77289",
"R-RNO-2142670",
"R-RNO-9018682",
"R-RNO-9033241",
"R-SSC-2142670",
"R-SSC-9018682",
"R-S... | [
"EC:3.1.3.76",
"EC:3.3.2.10",
"METACYC:PWY-6710",
"METACYC:PWY-7778",
"METACYC:PWY-8356",
"METACYC:PWY-8395",
"METACYC:PWY-8397",
"METACYC:PWY-8399",
"METACYC:PWY-8400",
"REACTOME:R-HSA-2142670",
"REACTOME:R-HSA-77289",
"REACTOME:R-HSA-9018682",
"REACTOME:R-HSA-9033241",
"REACTOME:R-MMU-77... | 20 | [
"1s8o",
"1vj5",
"1zd2",
"1zd3",
"1zd4",
"1zd5",
"3i1y",
"3i28",
"3koo",
"3otq",
"3wk4",
"3wk5",
"3wk6",
"3wk7",
"3wk8",
"3wk9",
"3wka",
"3wkb",
"3wkc",
"3wkd",
"3wke",
"4hai",
"4j03",
"4ocz",
"4od0",
"4y2j",
"4y2p",
"4y2q",
"4y2r",
"4y2s",
"4y2t",
"4y2u"... | 103 | [
"PUB00003337",
"PUB00015515"
] | [
"7966317",
"12574508"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
] | [
1994,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
382,
1660,
49
] | 3 | [
"Caenorhabditis elegans",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
4,
7,
2,
10
] | 4 | true | Domain | Predicted HAD-superfamily phosphatase, subfamily IA/Epoxide hydrolase, N-terminal | Predicted HAD-superfamily phosphatase, subfamily IA/Epoxide hydrolase, N-terminal | HAD-SF_ppase_IA/epoxid_hydro_N | 5 |
IPR011946 | 11,946 | Integrase, integron-type | Integrase_integron-type | Family | 3,347 | false | false | Members of this family are integrases associated with integrons (and super-integrons), which are systems for incorporating and expressing cassettes of laterally transferred DNA. Incorporation occurs at an attI site. A super-integron, as in Vibrio species, may include over 100 cassettes. This family belongs to the phage... | [
"GO:0003677",
"GO:0006310",
"GO:0015074"
] | [
"DNA binding",
"DNA recombination",
"DNA integration"
] | [
"molecular_function",
"biological_process",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR02249"
] | [
"integrase_gron"
] | [
3347
] | 1 | [
"GP"
] | [
"GenProp0226"
] | [
"GP:GenProp0226"
] | 1 | [
"2a3v"
] | 1 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Argoarchaeum ethanivorans",
"Caudoviricetes",
"Podocopida",
"plasmids",
"unclassified sequences"
] | [
3254,
1,
3,
3,
2,
84
] | 6 | [] | [] | 0 | true | Family | Integrase, integron-type | Integrase, integron-type | Integrase_integron-type | 1 |
IPR011947 | 11,947 | FCP1-like phosphatase, phosphatase domain | FCP1_euk | Domain | 5,774 | false | false | This entry represents the phosphatase domain of the human RNA polymerase II subunit A C-terminal domain phosphatase (FCP1, [ ]) and closely related phosphatases from eukaryotes including plants, fungi [ ] and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set... | [
"GO:0004721",
"GO:0005634"
] | [
"phosphoprotein phosphatase activity",
"nucleus"
] | [
"molecular_function",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02250"
] | [
"FCP1_euk"
] | [
5774
] | 1 | [
"EC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
... | [
"3.1.3.16",
"R-CEL-112382",
"R-CEL-113418",
"R-CEL-674695",
"R-CEL-6796648",
"R-CEL-75955",
"R-HSA-112382",
"R-HSA-113418",
"R-HSA-167152",
"R-HSA-167158",
"R-HSA-167200",
"R-HSA-167238",
"R-HSA-167242",
"R-HSA-167243",
"R-HSA-167246",
"R-HSA-167287",
"R-HSA-167290",
"R-HSA-674695"... | [
"EC:3.1.3.16",
"REACTOME:R-CEL-112382",
"REACTOME:R-CEL-113418",
"REACTOME:R-CEL-674695",
"REACTOME:R-CEL-6796648",
"REACTOME:R-CEL-75955",
"REACTOME:R-HSA-112382",
"REACTOME:R-HSA-113418",
"REACTOME:R-HSA-167152",
"REACTOME:R-HSA-167158",
"REACTOME:R-HSA-167200",
"REACTOME:R-HSA-167238",
"R... | 31 | [
"3ef0",
"3ef1",
"4xpz",
"4xq0"
] | 4 | [
"PUB00003337",
"PUB00009589",
"PUB00015516",
"PUB00015517"
] | [
"7966317",
"11601995",
"15170348",
"14701811"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases.",
"An encephalit... | [
1994,
2001,
2004,
2004
] | 4 | [
"IPR004274"
] | [] | 1 | 0 | 1 | [
"Eukaryota"
] | [
5774
] | 1 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
47,
1,
2,
2,
4,
2,
1,
9,
3,
1,
1,
21
] | 12 | true | Domain | FCP1-like phosphatase, phosphatase domain | FCP1-like phosphatase, phosphatase domain | FCP1_euk | 7 |
IPR011949 | 11,949 | HAD-superfamily hydrolase, subfamily IA, REG-2-like | HAD-SF_hydro_IA_REG-2-like | Family | 3,652 | false | false | This family of proteins includes uncharacterised sequences from eukaryotes, cyanobacteria and Leptospira as well as the DREG-2 protein from Drosophila melanogaster (Fruit fly) which has been identified as a rhythmically (diurnally) regulated gene [ ]. This family is a member of the Haloacid Dehalogenase (HAD) superfami... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02252"
] | [
"DREG-2"
] | [
3652
] | 1 | [] | [] | [] | 0 | [
"3k1z"
] | 1 | [
"PUB00003337",
"PUB00009540",
"PUB00015520"
] | [
"7966317",
"10956028",
"8749395"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and ca... | [
1994,
2000,
1995
] | 3 | [
"IPR006439"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"ecological metagenomes"
] | [
476,
3169,
7
] | 3 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)",
"Schizosaccharomyces pombe (strain 972 / ATCC 24843)",
"Zea ma... | [
9,
1,
1,
4,
2,
1,
10,
2,
1,
1,
14
] | 11 | true | Family | HAD-superfamily hydrolase, subfamily IA, REG-2-like | HAD-superfamily hydrolase, subfamily IA, REG-2-like | HAD-SF_hydro_IA_REG-2-like | 9 |
IPR011950 | 11,950 | HAD-superfamily hydrolase, subfamily IA, CTE7 | HAD-SF_hydro_IA_CTE7 | Family | 968 | false | false | This family of sequences from archaea and metazoans includes N-acylneuraminate-9-phosphatase Nanp from metazoa [ ] and glyceraldehyde 3-phosphate phosphatases from archaea [ ]. Pyrococcus species appear to have three different forms of this enzyme, so it is unclear whether all members of this family have the same funct... | [
"GO:0016787"
] | [
"hydrolase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02253"
] | [
"CTE7"
] | [
968
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"... | [
"3.1.3.-",
"GenProp1737",
"PWY-4702",
"PWY-5491",
"PWY-6148",
"PWY-6352",
"PWY-6365",
"PWY-6366",
"PWY-6368",
"PWY-6456",
"PWY-6575",
"PWY-6627",
"PWY-6664",
"PWY-6686",
"PWY-6720",
"PWY-6724",
"PWY-6955",
"PWY-6990",
"PWY-6991",
"PWY-7018",
"PWY-7119",
"PWY-7321",
"PWY-7... | [
"EC:3.1.3.-",
"GP:GenProp1737",
"METACYC:PWY-4702",
"METACYC:PWY-5491",
"METACYC:PWY-6148",
"METACYC:PWY-6352",
"METACYC:PWY-6365",
"METACYC:PWY-6366",
"METACYC:PWY-6368",
"METACYC:PWY-6456",
"METACYC:PWY-6575",
"METACYC:PWY-6627",
"METACYC:PWY-6664",
"METACYC:PWY-6686",
"METACYC:PWY-672... | 40 | [
"1x42",
"2gfh",
"2hoq",
"2w4m",
"3u26",
"4ffd",
"4knv",
"4knw",
"4ygq",
"4ygr",
"4ygs",
"6q7n",
"6q7o",
"6q7p",
"6q7q",
"6q7r",
"6z1k",
"6z1l",
"7o1d",
"8bp0",
"8bp1",
"9eqd",
"9fug",
"9ful",
"9fuo"
] | 25 | [
"PUB00003337",
"PUB00077113",
"PUB00077549"
] | [
"7966317",
"16237198",
"25848029"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase.",
"Panoramic view of a superfamily of phosph... | [
1994,
2006,
2015
] | 3 | [
"IPR006439"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eumetazoa",
"ecological metagenomes"
] | [
219,
21,
721,
7
] | 4 | [
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Rattus norvegicus"
] | [
1,
1,
1,
1,
4
] | 5 | true | Family | HAD-superfamily hydrolase, subfamily IA, CTE7 | HAD-superfamily hydrolase, subfamily IA, CTE7 | HAD-SF_hydro_IA_CTE7 | 2 |
IPR011951 | 11,951 | HAD-superfamily hydrolase, subfamily IA, YjjG/PynA | HAD-SF_hydro_IA_YjjG/PynA | Family | 7,238 | false | false | This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterised by three conserved sequence motifs [ ]. It includes pyrimidine 5'-nucleotidase YjjG from E. coli, pyrimidine 5'-nucleotidase PynA from Streptococcus pneumoniae and the uncharacterised protein YfnB from B. subtil... | [
"GO:0008253"
] | [
"5'-nucleotidase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02254"
] | [
"YjjG_YfnB"
] | [
7238
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"3.1.3.5",
"PWY-5381",
"PWY-5695",
"PWY-6596",
"PWY-6606",
"PWY-6607",
"PWY-6608",
"PWY-7185",
"PWY-7821"
] | [
"EC:3.1.3.5",
"METACYC:PWY-5381",
"METACYC:PWY-5695",
"METACYC:PWY-6596",
"METACYC:PWY-6606",
"METACYC:PWY-6607",
"METACYC:PWY-6608",
"METACYC:PWY-7185",
"METACYC:PWY-7821"
] | 9 | [
"3ed5",
"3i76",
"3qnm"
] | 3 | [
"PUB00003337",
"PUB00070801",
"PUB00097232"
] | [
"7966317",
"17286574",
"31437335"
] | [
"Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.",
"The Escherichia coli protein YjjG is a house-cleaning nucleotidase in vivo.",
"PynA is a pyrimidine 5'-nucleotidase that function... | [
1994,
2007,
2020
] | 3 | [
"IPR006439"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Heimdallarchaeum",
"Eukaryota",
"metagenomes"
] | [
7190,
2,
9,
37
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | HAD-superfamily hydrolase, subfamily IA, YjjG/PynA | HAD-superfamily hydrolase, subfamily IA, YjjG/PynA | HAD-SF_hydro_IA_YjjG/PynA | 9 |
IPR011953 | 11,953 | Cobaltochelatase, CobN subunit | Cobalto_CobN | Family | 5,771 | false | false | This family of proteins catalyzes the insertion of cobalt into the corrin ring of hydrogenobyrinic acid a,c-diamide. This aerobic branch of corrin ring synthesis is part of the adenosylcobalamin biosynthetic pathway [ ]. | [
"GO:0051116",
"GO:0009236"
] | [
"cobaltochelatase activity",
"cobalamin biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02257"
] | [
"cobalto_cobN"
] | [
5771
] | 1 | [] | [] | [] | 0 | [
"7c6o"
] | 1 | [
"PUB00009664"
] | [
"1429466"
] | [
"Assay, purification, and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriati",
"unclassified sequences"
] | [
5497,
5,
245,
24
] | 4 | [] | [] | 0 | true | Family | Cobaltochelatase, CobN subunit | Cobaltochelatase, CobN subunit | Cobalto_CobN | 4 |
IPR011954 | 11,954 | Benzoyl-CoA reductase, subunit A | Benzoyl_CoA_Rdtase_A | Family | 67 | false | false | This entry describes A subunit of benzoyl-CoA reductase, a 4-subunit enzyme [ ]. Many aromatic compounds are metabolized by way of benzoyl-CoA. This family shows strong sequence similarity to the 2-hydroxyglutaryl-CoA dehydratase alpha chain. | [
"GO:0018522"
] | [
"benzoyl-CoA reductase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02259"
] | [
"benz_CoA_red_A"
] | [
67
] | 1 | [
"GP"
] | [
"GenProp0702"
] | [
"GP:GenProp0702"
] | 1 | [] | 0 | [
"PUB00083916"
] | [
"8575453"
] | [
"Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thauera aromatica strain K172."
] | [
1995
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"ecological metagenomes"
] | [
62,
5
] | 2 | [] | [] | 0 | true | Family | Benzoyl-CoA reductase, subunit A | Benzoyl-CoA reductase, subunit A | Benzoyl_CoA_Rdtase_A | 6 |
IPR011955 | 11,955 | Benzoyl-CoA reductase, subunit B | Benzoyl_CoA_Rdtase_B | Family | 64 | false | false | This entry describes describes the B, or beta, subunit of the bcr type of benzoyl-CoA reductase, a 4-subunit enzyme. Many aromatic compounds are metabolised by way of benzoyl-CoA. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02260"
] | [
"benz_CoA_red_B"
] | [
64
] | 1 | [
"GP"
] | [
"GenProp0702"
] | [
"GP:GenProp0702"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR010327"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"ecological metagenomes"
] | [
58,
6
] | 2 | [] | [] | 0 | true | Family | Benzoyl-CoA reductase, subunit B | Benzoyl-CoA reductase, subunit B | Benzoyl_CoA_Rdtase_B | 1 |
IPR011956 | 11,956 | Benzoyl-CoA reductase, subunit D | Benzoyl_CoA_Rdtase_D | Family | 70 | false | false | This entry describes the D subunit of benzoyl-CoA reductase, a 4-subunit enzyme. Many aromatic compounds are metabolised by way of benzoyl-CoA. This family shows sequence similarity to the A subunit ( ) and to the 2-hydroxyglutaryl-CoA dehydratase alpha chain. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02261"
] | [
"benz_CoA_red_D"
] | [
70
] | 1 | [
"GP"
] | [
"GenProp0702"
] | [
"GP:GenProp0702"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"ecological metagenomes"
] | [
65,
5
] | 2 | [] | [] | 0 | true | Family | Benzoyl-CoA reductase, subunit D | Benzoyl-CoA reductase, subunit D | Benzoyl_CoA_Rdtase_D | 5 |
IPR011957 | 11,957 | Benzoate-CoA ligase family | Benz_CoA_lig | Family | 2,285 | false | false | Characterised members of this protein family include benzoate-CoA ligase [ ], 4-hydroxybenzoate-CoA ligase [ ], 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases. | [
"GO:0005524",
"GO:0016405"
] | [
"ATP binding",
"CoA-ligase activity"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02262"
] | [
"benz_CoA_lig"
] | [
2285
] | 1 | [] | [] | [] | 0 | [
"2v7b",
"4eat",
"4rlf",
"4rlq",
"4rm2",
"4rm3",
"4rmn",
"4wv3",
"4zjz",
"6m2o",
"6m2t",
"6m2u"
] | 12 | [
"PUB00078892",
"PUB00078893"
] | [
"11208796",
"12897012"
] | [
"Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium Thauera aromatica.",
"Benzoate-coenzyme A ligase from Thauera aromatica: an enzyme acting in anaerobic and aerobic pathways."
] | [
2001,
2003
] | 2 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
50,
2203,
3,
29
] | 4 | [] | [] | 0 | true | Family | Benzoate-CoA ligase family | Benzoate-CoA ligase family | Benz_CoA_lig | 2 |
IPR011958 | 11,958 | Benzoyl-CoA reductase, subunit C | Benzoyl_CoA_Rdtase_C | Family | 70 | false | false | This entry describes C subunit of benzoyl-CoA reductase, a 4-subunit enzyme. Many aromatic compounds are metabolised by way of benzoyl-CoA. This enzyme acts under anaerobic conditions. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02263"
] | [
"benz_CoA_red_C"
] | [
70
] | 1 | [
"GP"
] | [
"GenProp0702"
] | [
"GP:GenProp0702"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR010327"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"ecological metagenomes"
] | [
63,
7
] | 2 | [] | [] | 0 | true | Family | Benzoyl-CoA reductase, subunit C | Benzoyl-CoA reductase, subunit C | Benzoyl_CoA_Rdtase_C | 3 |
IPR011959 | 11,959 | Conserved hypothetical protein CHP02270 | CHP02270 | Family | 390 | false | false | Members are found in Myxococcus xanthus (six members), Geobacter sulfurreducens, and Pseudomonas aeruginosa; a short protein homologous to the N-terminal region is found in Rhizobium loti (Mesorhizobium loti). All sequence are from Proteobacteria. The function is unknown. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02270"
] | [
""
] | [
390
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"metagenomes"
] | [
375,
15
] | 2 | [] | [] | 0 | true | Family | Conserved hypothetical protein CHP02270 | Conserved hypothetical protein CHP02270 | CHP02270 | 2 |
IPR011960 | 11,960 | Gentisate 1,2 dioxygenase 1 | Gentisate_dOase | Family | 1,354 | false | false | This family consists of gentisate 1,2-dioxygenases, including Gentisate 1,2 dioxygenase 1 from Pseudomonas alcaligenes [ , ] that exhibits broad substrate specificities towards alkyl and halogenated gentisates. These ring-opening enzymes acts in salicylate degradation that goes via gentisate rather than via catechol. I... | [
"GO:0047922"
] | [
"gentisate 1,2-dioxygenase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02272"
] | [
"gentisate_1_2"
] | [
1354
] | 1 | [] | [] | [] | 0 | [
"2d40"
] | 1 | [
"PUB00097233",
"PUB00097234"
] | [
"16237038",
"10049846"
] | [
"Replacement of tyrosine 181 by phenylalanine in gentisate 1,2-dioxygenase I from Pseudomonas alcaligenes NCIMB 9867 enhances catalytic activities.",
"Purification and characterization of gentisate 1,2-dioxygenases from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869."
] | [
2005,
1999
] | 2 | [
"IPR047183"
] | [] | 1 | 0 | 1 | [
"Anopheles maculatus",
"Bacteria",
"marine metagenome"
] | [
1,
1349,
4
] | 3 | [] | [] | 0 | true | Family | Gentisate 1,2 dioxygenase 1 | Gentisate 1,2 dioxygenase 1 | Gentisate_dOase | 3 |
IPR011961 | 11,961 | Ribosome maturation factor RimM | RimM | Family | 24,760 | false | false | This family consists of the bacterial protein RimM (YfjA, 21K), a 30S ribosomal subunit-binding protein implicated in 16S ribosomal RNA processing. It has been partially characterised in Escherichia coli, is found with other translation-associated genes such as trmD. It is broadly distributed among bacteria, including ... | [
"GO:0043022",
"GO:0006364",
"GO:0005840"
] | [
"ribosome binding",
"rRNA processing",
"ribosome"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"PANTHER",
"NCBIFAM"
] | [
"MF_00014",
"PTHR33692",
"TIGR02273"
] | [
"Ribosome_mat_RimM",
"",
"16S_RimM"
] | [
24379,
24200,
24288
] | 3 | [
"GP"
] | [
"GenProp0802"
] | [
"GP:GenProp0802"
] | 1 | [
"2dyi",
"2f1l",
"2qgg",
"3a1p",
"3h9n",
"7cq1"
] | 6 | [
"PUB00002319"
] | [
"9422595"
] | [
"RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Escherichia phage vB_EcoM-613R3",
"Eukaryota",
"candidate division MSBL1 archaeon SCGC-AAA382M17",
"unclassified sequences"
] | [
23416,
1,
845,
1,
497
] | 5 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
4,
1,
3,
15
] | 4 | true | Family | Ribosome maturation factor RimM | Ribosome maturation factor RimM | RimM | 7 |
IPR011962 | 11,962 | dCTP deaminase | dCTP_deaminase | Family | 17,520 | false | false | Deoxycytidine triphosphate deaminase (dCTP deaminase) is an enzyme involved in nucleotide metabolism. It catalyses the formation of dUTP (deoxyuridine (5'-)triphosphate), which in turn is degraded by dUTPase (dUTP diphosphatase) to produce dUMP (deoxyuridine monophosphate). dUMP is the immediate precursor of thymidine ... | [
"GO:0008829",
"GO:0006229"
] | [
"dCTP deaminase activity",
"dUTP biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"PFAM",
"NCBIFAM"
] | [
"MF_00146",
"PF22769",
"TIGR02274"
] | [
"dCTP_deaminase",
"DCD",
"dCTP_deam"
] | [
13195,
17520,
15164
] | 3 | [
"EC",
"GP",
"METACYC"
] | [
"3.5.4.13",
"GenProp1621",
"PWY-7187"
] | [
"EC:3.5.4.13",
"GP:GenProp1621",
"METACYC:PWY-7187"
] | 3 | [
"1ogh",
"1pkh",
"1pkj",
"1pkk",
"1xs1",
"1xs4",
"1xs6",
"2hxb",
"2hxd",
"2j4h",
"2j4q",
"2qlp",
"2qxx",
"2v9x",
"2yzj",
"2zdc",
"3gf0",
"3km3",
"4a6a",
"4dhk",
"4xjc",
"8y1w"
] | 22 | [
"PUB00006279",
"PUB00029426",
"PUB00038355",
"PUB00043996",
"PUB00049054",
"PUB00049646",
"PUB00080261"
] | [
"1324907",
"12756253",
"15539408",
"17651436",
"18164314",
"17996716",
"12538648"
] | [
"dcd (dCTP deaminase) gene of Escherichia coli: mapping, cloning, sequencing, and identification as a locus of suppressors of lethal dut (dUTPase) mutations.",
"Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases.",
"Structures ... | [
1992,
2003,
2005,
2007,
2008,
2008,
2003
] | 7 | [] | [
"IPR023537"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
1378,
15123,
413,
201,
405
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | dCTP deaminase | dCTP deaminase | dCTP_deaminase | 8 |
IPR011963 | 11,963 | 2,3-dihydroxybenzoate-AMP ligase | DHB_AMP_lig | Family | 2,910 | false | false | Siderophores are low molecular weight iron-chelating compounds synthesised by many bacteria to aid in the aquisition of this vital trace element [ ]. Proteins in this entry are adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores. These proteins belong to the AM... | [
"GO:0008668",
"GO:0019290"
] | [
"2,3-dihydroxybenzoate--[aryl-carrier protein] ligase activity",
"siderophore biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02275"
] | [
"DHB_AMP_lig"
] | [
2910
] | 1 | [
"EC"
] | [
"6.2.1.71"
] | [
"EC:6.2.1.71"
] | 1 | [
"1md9",
"1mdb",
"1mdf",
"3o82",
"3o83",
"3o84",
"3rg2",
"3u16",
"3u17",
"4iz6",
"6e8o",
"6e97",
"6iyk",
"6iyl",
"8k5s",
"8k5t",
"9my5",
"9my6",
"9my7"
] | 19 | [
"PUB00005277",
"PUB00022164",
"PUB00028109",
"PUB00054028"
] | [
"8805533",
"12221282",
"11018148",
"2531000"
] | [
"Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes.",
"Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases.",
"Iron metabolism in pathogenic bacteria.",
"Subcloning, expression, and purification o... | [
1996,
2002,
2000,
1989
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Timema poppense"
] | [
2909,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 2,3-dihydroxybenzoate-AMP ligase | 2,3-dihydroxybenzoate-AMP ligase | DHB_AMP_lig | 2 |
IPR011964 | 11,964 | YVTN beta-propeller repeat | YVTN_b-propeller_repeat | Repeat | 12,412 | false | false | This entry represents a repeat of about 40 amino acids found in a variety of archaea and bacteria which can be present in up to 14 copies per protein. The archaeal species Methanosarcina mazei (Methanosarcina frisia) contains several predicted surface layer proteins (SLPs) containing tandem copies of this repeat [ ]. T... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02276"
] | [
"beta_rpt_yvtn"
] | [
12412
] | 1 | [] | [] | [] | 0 | [
"1l0q",
"5c2v",
"5c2w"
] | 3 | [
"PUB00014157"
] | [
"12377130"
] | [
"Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
531,
11564,
29,
288
] | 4 | [] | [] | 0 | true | Repeat | YVTN beta-propeller repeat | YVTN beta-propeller repeat | YVTN_b-propeller_repeat | 3 |
IPR011965 | 11,965 | Phenylacetic acid degradation operon negative regulatory protein PaaX | PaaX_trns_reg | Family | 6,967 | false | false | This transcriptional regulator is always found in association with operons believed to be involved in the degradation of phenylacetic acid [ ]. The gene product has been shown to bind to the promoter sites and repress their transcription [ ]. | [
"GO:0006351"
] | [
"DNA-templated transcription"
] | [
"biological_process"
] | 1 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF020623",
"TIGR02277"
] | [
"PaaX",
"PaaX_trns_reg"
] | [
6962,
1774
] | 2 | [] | [] | [] | 0 | [
"8a39"
] | 1 | [
"PUB00015494",
"PUB00015522"
] | [
"11260461",
"10766858"
] | [
"The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications.",
"Transcriptional regulation of the divergent paa catabolic operons for phenylacetic acid degradation in Escherichia coli."
] | [
2001,
2000
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5",
"Sulfolobaceae",
"unclassified sequences"
] | [
6887,
1,
31,
48
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phenylacetic acid degradation operon negative regulatory protein PaaX | Phenylacetic acid degradation operon negative regulatory protein PaaX | PaaX_trns_reg | 9 |
IPR011966 | 11,966 | Phenylacetic acid degradation protein PaaN | PaaN-DH | Family | 4,061 | false | false | This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation [ ] which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardised in [ ]. This enzyme is related to aldehyde deh... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR02278"
] | [
"PaaN-DH"
] | [
4061
] | 1 | [] | [] | [] | 0 | [
"2vro",
"6jql",
"6jqm",
"6jqn",
"6jqo",
"8pvi",
"8wv6"
] | 7 | [
"PUB00010200",
"PUB00015494"
] | [
"9748275",
"11260461"
] | [
"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.",
"The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications."
] | [
1998,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4040,
5,
16
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phenylacetic acid degradation protein PaaN | Phenylacetic acid degradation protein PaaN | PaaN-DH | 5 |
IPR011967 | 11,967 | 3-hydroxyadipyl-CoA dehydrogenase PaaH | 3-OHacyl-CoA_DH_PaaH | Family | 795 | false | false | This entry represents the 3-hydroxyacyl-CoA dehydrogenase (also known as PaaH) and related bacterial proteins. PaaH is involved in the degradation of phenylacetic acid, presumably in steps following the opening of the phenyl ring [ ]. The sequences included in this entry are all found in possible operons with other rel... | [
"GO:0008691",
"GO:0010124"
] | [
"3-hydroxybutyryl-CoA dehydrogenase activity",
"phenylacetate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR02279"
] | [
"PaaC-3OHAcCoADH"
] | [
795
] | 1 | [] | [] | [] | 0 | [
"3mog"
] | 1 | [
"PUB00010200",
"PUB00015494"
] | [
"9748275",
"11260461"
] | [
"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.",
"The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications."
] | [
1998,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Pseudomonadati",
"unclassified sequences"
] | [
792,
3
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 3-hydroxyadipyl-CoA dehydrogenase PaaH | 3-hydroxyadipyl-CoA dehydrogenase PaaH | 3-OHacyl-CoA_DH_PaaH | 4 |
IPR011968 | 11,968 | Phenylacetate degradation probable enoyl-CoA hydratase PaaB | PaaB1 | Family | 2,426 | false | false | This family of proteins are found within apparent operons for the degradation of phenylacetic acid [ ]. These proteins contain the enoyl-CoA hydratase domain. This activity is consistent with current hypotheses for the degradation pathway [ ] which involve the ligation of phenylacetate with coenzyme A (paaF), hydroxyla... | [
"GO:0010124"
] | [
"phenylacetate catabolic process"
] | [
"biological_process"
] | 1 | [
"NCBIFAM"
] | [
"TIGR02280"
] | [
"PaaB1"
] | [
2426
] | 1 | [] | [] | [] | 0 | [
"4fzw"
] | 1 | [
"PUB00010200",
"PUB00015494"
] | [
"9748275",
"11260461"
] | [
"Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway.",
"The phenylacetyl-CoA catabolon: a complex catabolic unit with broad biotechnological applications."
] | [
1998,
2001
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Beauveria bassiana D1-5",
"unclassified sequences"
] | [
2412,
1,
13
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phenylacetate degradation probable enoyl-CoA hydratase PaaB | Phenylacetate degradation probable enoyl-CoA hydratase PaaB | PaaB1 | 5 |
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