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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR023942",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0000287",
"name": "magnesium ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0033982",
"name": "3-dehydro-L-gulonate-6-phosphate decarboxylase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0019854",
"name": "L-ascorbic acid catabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"hamap": {
"MF_01267": "3-keto-L-gulonate-6-phosphate decarboxylase UlaD [ulaD]"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR023942",
"name": "3-keto-L-gulonate-6-phosphate decarboxylase, UlaD",
"type": "Family",
"children": []
},
"name": {
"name": "3-keto-L-gulonate-6-phosphate decarboxylase, UlaD",
"short": "3-keto-L-gulonate6Pdecase_UlaD"
},
"description": [
{
"text": "<p>3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) ([ec:4.1.1.85]) is encoded by the ulaD gene in Escherichia coli [[cite:PUB00009905]]. The enzyme catalyses the decarboxylation of 3-keto-L-gulonate-6-phosphate into L-xylulose-5-phosphate, and may be involved in anaerobic L-ascorbate utilisation [[cite:PUB00009905]]. KGPDC is a homodimer of (β/α)8-barrels, with the active sites located at the dimer interface [[cite:PUB00026830]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00026830": {
"PMID": 11900527,
"ISBN": null,
"volume": "41",
"issue": "12",
"year": 2002,
"title": "Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase.",
"URL": null,
"raw_pages": "3861-9",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Wise E",
"Yew WS",
"Babbitt PC",
"Gerlt JA",
"Rayment I."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi012174e"
},
"PUB00009905": {
"PMID": 11741871,
"ISBN": null,
"volume": "184",
"issue": "1",
"year": 2002,
"title": "Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons.",
"URL": null,
"raw_pages": "302-6",
"medline_journal": "J Bacteriol",
"ISO_journal": "J. Bacteriol.",
"authors": [
"Yew WS",
"Gerlt JA."
],
"DOI_URL": "http://dx.doi.org/10.1128/JB.184.1.302-306.2002"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR011060",
"name": "Ribulose-phosphate binding barrel",
"type": "homologous_superfamily"
},
{
"accession": "IPR013785",
"name": "Aldolase-type TIM barrel",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 449,
"pathways": 1,
"proteins": 449,
"proteomes": 28,
"sets": 0,
"structural_models": {
"alphafold": 440,
"bfvd": 0
},
"structures": 14,
"taxa": 370
},
"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": "4.1.1.85",
"url": "https://enzyme.expasy.org/EC/4.1.1.85"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1q6o",
"name": "Structure of 3-keto-L-gulonate 6-phosphate decarboxylase with bound L-gulonaet 6-phosphate"
}
}
}
