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{
"metadata": {
"accession": "PF05681",
"entry_id": null,
"type": "family",
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"source_database": "pfam",
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"integrated": "IPR004646",
"hierarchy": null,
"name": {
"name": "Fumarate hydratase (Fumerase)",
"short": "Fumerase"
},
"description": [
{
"text": "<p>This family consists of several bacterial fumarate hydratase proteins FumA and FumB. Fumarase, or fumarate hydratase (EC 4.2.1.2), is a component of the citric acid cycle. In facultative anaerobes such as Escherichia coli, fumarase also engages in the reductive pathway from oxaloacetate to succinate during anaerobic growth. Three fumarases, FumA, FumB, and FumC, have been reported in E. coli. fumA and fumB genes are homologous and encode products of identical sizes which form thermolabile dimers of Mr 120,000. FumA and FumB are class I enzymes and are members of the iron-dependent hydrolases, which include aconitase and malate hydratase. The active FumA contains a 4Fe-4S centre, and it can be inactivated upon oxidation to give a 3Fe-4S centre [[cite:PUB00011340]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": [
{
"title": "Fumarase",
"extract": "<p><b>Fumarase</b> is an enzyme that catalyzes the reversible hydration/dehydration of fumarate to malate. Fumarase comes in two forms: mitochondrial and cytosolic. The mitochondrial isoenzyme is involved in the Krebs cycle and the cytosolic isoenzyme is involved in the metabolism of amino acids and fumarate. Subcellular localization is established by the presence of a signal sequence on the amino terminus in the mitochondrial form, while subcellular localization in the cytosolic form is established by the absence of the signal sequence found in the mitochondrial variety.</p>",
"thumbnail": null
}
],
"literature": {
"PUB00011340": {
"PMID": 11133938,
"ISBN": null,
"volume": "183",
"issue": "2",
"year": 2001,
"title": "Oxygen- and growth rate-dependent regulation of Escherichia coli fumarase (FumA, FumB, and FumC) activity.",
"URL": null,
"raw_pages": "461-7",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Tseng CP",
"Yu CC",
"Lin HH",
"Chang CY",
"Kuo JT."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.183.2.461-467.2001"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 20,
"interactions": 0,
"matches": 19415,
"pathways": 0,
"proteins": 19368,
"proteomes": 10285,
"sets": 0,
"structural_models": {
"alphafold": 15358,
"bfvd": 0
},
"structures": 17,
"taxa": 17528
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 250,
"alignment:full": 6028
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
