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{
"metadata": {
"accession": "IPR003473",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0008987",
"name": "quinolinate synthetase A activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0051539",
"name": "4 iron, 4 sulfur cluster binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0009435",
"name": "NAD+ biosynthetic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR30573": "QUINOLINATE SYNTHETASE A"
},
"pfam": {
"PF02445": "Quinolinate synthetase A protein"
},
"ncbifam": {
"TIGR00550": "quinolinate synthase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR003473",
"name": "Quinolinate synthetase A",
"type": "Family",
"children": [
{
"accession": "IPR023066",
"name": "Quinolinate synthase A, type 2",
"type": "Family",
"children": []
},
{
"accession": "IPR023513",
"name": "Quinolinate synthase A, type 1",
"type": "Family",
"children": []
},
{
"accession": "IPR023515",
"name": "Quinolinate synthase A, type 3",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Quinolinate synthetase A",
"short": "NadA"
},
"description": [
{
"text": "<p>Quinolinate synthetase catalyses the second step of the<i>de novo</i>biosynthetic pathway of pyridine nucleotide formation. In particular, quinolinate synthetase is involved in the condensation of dihydroxyacetone phosphate and iminoaspartate to form quinolinic acid [[cite:PUB00009471]]. This synthesis requires two enzymes, an FAD-containing \"B protein\" and an \"A protein\". B protein converts L-aspartate to iminoaspartate. The A protein, NadA, converts iminoaspartate to quinolate. NadA harbours a [4Fe-4S] cluster [[cite:PUB00070332]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00009471": {
"PMID": 10648170,
"ISBN": null,
"volume": "18",
"issue": "1",
"year": 2000,
"title": "Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase.",
"URL": null,
"raw_pages": "64-70",
"medline_journal": "Protein Expr Purif",
"ISO_journal": "Protein Expr. Purif.",
"authors": [
"Ceciliani F",
"Caramori T",
"Ronchi S",
"Tedeschi G",
"Mortarino M",
"Galizzi A."
],
"DOI_URL": "http://dx.doi.org/10.1006/prep.1999.1153"
},
"PUB00070332": {
"PMID": 18803397,
"ISBN": null,
"volume": "47",
"issue": "41",
"year": 2008,
"title": "Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes.",
"URL": null,
"raw_pages": "10999-1012",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Saunders AH",
"Griffiths AE",
"Lee KH",
"Cicchillo RM",
"Tu L",
"Stromberg JA",
"Krebs C",
"Booker SJ."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi801268f"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036094",
"name": "Quinolinate synthetase A superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 38,
"interactions": 0,
"matches": 20780,
"pathways": 4,
"proteins": 20777,
"proteomes": 13550,
"sets": 0,
"structural_models": {
"alphafold": 16093,
"bfvd": 0
},
"structures": 30,
"taxa": 22982
},
"entry_annotations": {
"alignment:seed": 380,
"alignment:full": 7419
},
"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": "GenProp0057",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0057"
}
]
},
"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": "2.5.1.72",
"url": "https://enzyme.expasy.org/EC/2.5.1.72"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "6nso",
"name": "An Unexpected Intermediate in the Reaction Catalyzed by Quinolinate Synthase"
}
}
}
