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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR011830",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0046912",
"name": "acyltransferase activity, acyl groups converted into alkyl on transfer",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0019752",
"name": "carboxylic acid metabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"ncbifam": {
"TIGR02090": "isopropylmalate/citramalate/homocitrate synthases"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR000891",
"name": "Pyruvate carboxyltransferase",
"type": "Domain",
"children": [
{
"accession": "IPR011830",
"name": "Isopropylmalate/citramalate/homocitrate synthase",
"type": "Domain",
"children": []
},
{
"accession": "IPR035685",
"name": "4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR039371",
"name": "LeuA, N-terminal catalytic TIM barrel domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR048253",
"name": "Homocitrate synthase, catalytic TIM barrel domain, fungi/bacteria",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "Isopropylmalate/citramalate/homocitrate synthase",
"short": "LEU1_arch"
},
"description": [
{
"text": "<p>Methanogenic archaea contain three closely related homologues of the 2-isopropylmalate synthases (LeuA) represented by [interpro:IPR005671]. Two of these in Methanococcus janaschii (MJ1392 - CimA [[cite:PUB00015474]]; MJ0503 - AksA [[cite:PUB00015475]]) have been characterised as catalyzing alternative reactions leaving the third (MJ1195) as the presumptive LeuA enzyme. CimA is citramalate (2-methylmalate) synthase, which condenses acetyl-CoA with pyruvate. This enzyme is believed to be involved in the biosynthesis of isoleucine in methanogens and possibly other species lacking threonine dehydratase. AksA is a homocitrate synthase which also produces (homo)2-citrate and (homo)3-citrate in the biosynthesis of Coenzyme B which is restricted solely to methanogenic archaea. Methanogens, then should and apparently do contain all three of these enzymes. Unfortunately, phylogenetic trees do not resolve into three unambiguous clades, making assignment of function to particular genes problematic. Other archaea, which lack a threonine dehydratase (mainly Euryarchaeota), should contain both CimA and LeuA genes. This is true for archaeoglobus fulgidis, but not for the Pyrococci which have none in this clade, but one in [interpro:IPR005671] and one in [interpro:IPR005675] which may fulfil these roles. Proteins from other species, which have only one hit to this entry and lack threonine dehydratase, are very likely to be LeuA enzymes.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00015474": {
"PMID": 9864346,
"ISBN": null,
"volume": "181",
"issue": "1",
"year": 1999,
"title": "(R)-citramalate synthase in methanogenic archaea.",
"URL": null,
"raw_pages": "331-3",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Howell DM",
"Xu H",
"White RH."
],
"DOI_URL": "http://jb.asm.org/cgi/content/abstract/181/1/331"
},
"PUB00015475": {
"PMID": 9665716,
"ISBN": null,
"volume": "37",
"issue": "28",
"year": 1998,
"title": "Alpha-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic Archaea.",
"URL": null,
"raw_pages": "10108-17",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Howell DM",
"Harich K",
"Xu H",
"White RH."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi980662p"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR013785",
"name": "Aldolase-type TIM barrel",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 687,
"pathways": 0,
"proteins": 687,
"proteomes": 235,
"sets": 0,
"structural_models": {
"alphafold": 649,
"bfvd": 0
},
"structures": 0,
"taxa": 627
},
"entry_annotations": {},
"cross_references": {
"gp": {
"displayName": "Genome Properties",
"description": "Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.",
"rank": 45,
"accessions": [
{
"accession": "GenProp0193",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0193"
},
{
"accession": "GenProp0164",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0164"
}
]
},
"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": "2.3.3",
"url": "https://enzyme.expasy.org/EC/2.3.3"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
