HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "IPR016039",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": [
{
"identifier": "GO:0016746",
"name": "acyltransferase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"cathgene3d": {
"G3DSA:3.40.47.10": "G3DSA:3.40.47.10"
},
"ssf": {
"SSF53901": "Thiolase-like"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR016039",
"name": "Thiolase-like",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "Thiolase-like",
"short": "Thiolase-like"
},
"description": [
{
"text": "<p>This superfamily represents a structural domain with a thiolase-like 3-layer α/β/α topology. This domain usually occurs in two similar copies that are related by a pseudo-dyad, and which arose through duplication. The proteins in this entry can be split into two groups: those related to thiolase, and those related to chalcone synthase. The thiolase-like enzymes include:</p>\n\n<ul>\n<li>Thiolase, where the topology of each domain is similar to the first domain of phosphoglucomutase [[cite:PUB00020434]]</li>\n<li>Beta-ketoacyl-ACP synthases types I ([ec:2.3.1.41]), II ([ec:2.3.1.179]) [[cite:PUB00036842], [cite:PUB00019762]] and III ([ec:2.3.1.180])</li>\n<li>Actinorhodin polyketide beta-ketoacyl synthases 1 and 2 [[cite:PUB00031547]]</li>\n<li>Fatty oxidation complex beta subunit (3-ketoacyl-CoA thiolase; [ec:2.3.1.16]) [[cite:PUB00032244]]</li>\n</ul>\n\n<p>The chalcone synthase-like enzymes include:</p>\n\n<ul>\n<li>Chalcone synthase ([ec:2.3.1.74]) [[cite:PUB00014381]]</li>\n<li>Ketoacyl-ACP synthase III (FabH; [ec:2.3.1.180]) [[cite:PUB00025721]]</li>\n<li>Polyketide synthases [[cite:PUB00031426]]</li>\n<li>3-hydroxy-3-methylglutaryl CoA synthase ([ec:2.3.3.10]) [[cite:PUB00016103]]</li>\n<li>Dihydropinosylvin synthase [[cite:PUB00031633]]</li>\n</ul>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00032244": {
"PMID": 15229654,
"ISBN": null,
"volume": "23",
"issue": "14",
"year": 2004,
"title": "Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.",
"URL": null,
"raw_pages": "2745-54",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Ishikawa M",
"Tsuchiya D",
"Oyama T",
"Tsunaka Y",
"Morikawa K."
],
"DOI_URL": "http://dx.doi.org/10.1038/sj.emboj.7600298"
},
"PUB00020434": {
"PMID": 9402066,
"ISBN": null,
"volume": "273",
"issue": "3",
"year": 1997,
"title": "The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism.",
"URL": null,
"raw_pages": "714-28",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Mathieu M",
"Modis Y",
"Zeelen JP",
"Engel CK",
"Abagyan RA",
"Ahlberg A",
"Rasmussen B",
"Lamzin VS",
"Kunau WH",
"Wierenga RK."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1997.1331"
},
"PUB00036842": {
"PMID": 16441657,
"ISBN": null,
"volume": "273",
"issue": "4",
"year": 2006,
"title": "Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases.",
"URL": null,
"raw_pages": "695-710",
"medline_journal": "FEBS J",
"ISO_journal": "FEBS J.",
"authors": [
"von Wettstein-Knowles P",
"Olsen JG",
"McGuire KA",
"Henriksen A."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1742-4658.2005.05101.x"
},
"PUB00019762": {
"PMID": 9482715,
"ISBN": null,
"volume": "17",
"issue": "5",
"year": 1998,
"title": "Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.",
"URL": null,
"raw_pages": "1183-91",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Huang W",
"Jia J",
"Edwards P",
"Dehesh K",
"Schneider G",
"Lindqvist Y."
],
"DOI_URL": "http://dx.doi.org/10.1093/emboj/17.5.1183"
},
"PUB00031547": {
"PMID": 15286722,
"ISBN": null,
"volume": "11",
"issue": "9",
"year": 2004,
"title": "An antibiotic factory caught in action.",
"URL": null,
"raw_pages": "888-93",
"medline_journal": "Nat Struct Mol Biol",
"ISO_journal": "Nat. Struct. Mol. Biol.",
"authors": [
"Keatinge-Clay AT",
"Maltby DA",
"Medzihradszky KF",
"Khosla C",
"Stroud RM."
],
"DOI_URL": "http://dx.doi.org/10.1038/nsmb808"
},
"PUB00014381": {
"PMID": 11732902,
"ISBN": null,
"volume": "40",
"issue": "49",
"year": 2001,
"title": "Structure-guided programming of polyketide chain-length determination in chalcone synthase.",
"URL": null,
"raw_pages": "14829-38",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Jez JM",
"Bowman ME",
"Noel JP."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi015621z"
},
"PUB00025721": {
"PMID": 11243824,
"ISBN": null,
"volume": "307",
"issue": "1",
"year": 2001,
"title": "Refined structures of beta-ketoacyl-acyl carrier protein synthase III.",
"URL": null,
"raw_pages": "341-56",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Qiu X",
"Janson CA",
"Smith WW",
"Head M",
"Lonsdale J",
"Konstantinidis AK."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.2000.4457"
},
"PUB00031426": {
"PMID": 15286723,
"ISBN": null,
"volume": "11",
"issue": "9",
"year": 2004,
"title": "A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites.",
"URL": null,
"raw_pages": "894-900",
"medline_journal": "Nat Struct Mol Biol",
"ISO_journal": "Nat. Struct. Mol. Biol.",
"authors": [
"Sankaranarayanan R",
"Saxena P",
"Marathe UB",
"Gokhale RS",
"Shanmugam VM",
"Rukmini R."
],
"DOI_URL": "http://dx.doi.org/10.1038/nsmb809"
},
"PUB00016103": {
"PMID": 15292254,
"ISBN": null,
"volume": "279",
"issue": "43",
"year": 2004,
"title": "Staphylococcus aureus 3-hydroxy-3-methylglutaryl-CoA synthase: crystal structure and mechanism.",
"URL": null,
"raw_pages": "44883-8",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Campobasso N",
"Patel M",
"Wilding IE",
"Kallender H",
"Rosenberg M",
"Gwynn MN."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M407882200"
},
"PUB00031633": {
"PMID": 15380179,
"ISBN": null,
"volume": "11",
"issue": "9",
"year": 2004,
"title": "An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases.",
"URL": null,
"raw_pages": "1179-94",
"medline_journal": "Chem Biol",
"ISO_journal": "Chem. Biol.",
"authors": [
"Austin MB",
"Bowman ME",
"Ferrer JL",
"Schroder J",
"Noel JP."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.chembiol.2004.05.024"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR002155",
"name": "Thiolase",
"type": "family"
},
{
"accession": "IPR012793",
"name": "Beta-ketoadipyl CoA thiolase",
"type": "family"
},
{
"accession": "IPR014030",
"name": "Beta-ketoacyl synthase-like, N-terminal domain",
"type": "domain"
},
{
"accession": "IPR000794",
"name": "Beta-ketoacyl synthase",
"type": "family"
},
{
"accession": "IPR014031",
"name": "Beta-ketoacyl synthase, C-terminal domain",
"type": "domain"
},
{
"accession": "IPR013751",
"name": "Beta-ketoacyl-[acyl-carrier-protein] synthase III, N-terminal",
"type": "domain"
},
{
"accession": "IPR013747",
"name": "Beta-ketoacyl-[acyl-carrier-protein] synthase III, C-terminal",
"type": "domain"
},
{
"accession": "IPR012805",
"name": "Acetyl-CoA C-acyltransferase FadA",
"type": "family"
},
{
"accession": "IPR001099",
"name": "Chalcone/stilbene synthase, N-terminal",
"type": "domain"
},
{
"accession": "IPR012328",
"name": "Chalcone/stilbene synthase, C-terminal",
"type": "domain"
},
{
"accession": "IPR011141",
"name": "Polyketide synthase, type III",
"type": "family"
},
{
"accession": "IPR013528",
"name": "Hydroxymethylglutaryl-coenzyme A synthase, N-terminal",
"type": "domain"
},
{
"accession": "IPR013746",
"name": "Hydroxymethylglutaryl-coenzyme A synthase, C-terminal domain",
"type": "domain"
},
{
"accession": "IPR010122",
"name": "Hydroxymethylglutaryl-CoA synthase, eukaryotic",
"type": "family"
},
{
"accession": "IPR004655",
"name": "Beta-ketoacyl-[acyl-carrier-protein] synthase III",
"type": "family"
},
{
"accession": "IPR010894",
"name": "Stage V sporulation AD",
"type": "family"
},
{
"accession": "IPR012806",
"name": "Acetyl-CoA C-acyltransferase FadI",
"type": "family"
},
{
"accession": "IPR012392",
"name": "Very-long-chain 3-ketoacyl-CoA synthase",
"type": "family"
},
{
"accession": "IPR013601",
"name": "FAE1/Type III polyketide synthase-like protein",
"type": "domain"
},
{
"accession": "IPR011554",
"name": "Hydroxymethylglutaryl-CoA synthase, prokaryotic",
"type": "family"
},
{
"accession": "IPR004656",
"name": "Hydroxymethylglutaryl-CoA synthase",
"type": "family"
},
{
"accession": "IPR020616",
"name": "Thiolase, N-terminal",
"type": "domain"
},
{
"accession": "IPR020617",
"name": "Thiolase, C-terminal",
"type": "domain"
},
{
"accession": "IPR050215",
"name": "3-ketoacyl-CoA thiolase-like",
"type": "family"
},
{
"accession": "IPR020841",
"name": "Polyketide synthase, beta-ketoacyl synthase domain",
"type": "domain"
},
{
"accession": "IPR050521",
"name": "3-ketoacyl-CoA Thiolase",
"type": "family"
},
{
"accession": "IPR032821",
"name": "Polyketide synthase, C-terminal extension",
"type": "domain"
},
{
"accession": "IPR017568",
"name": "3-oxoacyl-[acyl-carrier-protein] synthase 2",
"type": "family"
},
{
"accession": "IPR055140",
"name": "Thiolase, C-terminal domain 2",
"type": "domain"
},
{
"accession": "IPR047224",
"name": "Fatty acid synthase subunit alpha-like, C-terminal",
"type": "domain"
},
{
"accession": "IPR046403",
"name": "3-oxopimeloyl-[acyl-carrier-protein] synthase",
"type": "family"
},
{
"accession": "IPR038369",
"name": "Stage V sporulation AD superfamily",
"type": "homologous_superfamily"
},
{
"accession": "IPR053528",
"name": "Thiolase-like Beta-ketothiolase",
"type": "family"
},
{
"accession": "IPR053446",
"name": "3,5-Dihydroxyphenylacetyl-CoA Synthase",
"type": "family"
},
{
"accession": "IPR049957",
"name": "Acetoacetyl-CoA reductase PhaA, cyanobacteria",
"type": "family"
},
{
"accession": "IPR053544",
"name": "HMG-CoA Synthase-like",
"type": "family"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 478251,
"pathways": 128,
"proteins": 438639,
"proteomes": 21021,
"sets": 0,
"structural_models": {
"alphafold": 285488,
"bfvd": 5
},
"structures": 836,
"taxa": 48542
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.3.1",
"url": "https://enzyme.expasy.org/EC/2.3.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "4yuc",
"name": "Crystal Structure of CorB derivatized with S-(2-acetamidoethyl) 4-methyl-3-oxohexanethioate"
}
}
}
