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{
"metadata": {
"accession": "IPR023210",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF00248": "Aldo/keto reductase family"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR023210",
"name": "NADP-dependent oxidoreductase domain",
"type": "Domain",
"children": []
},
"name": {
"name": "NADP-dependent oxidoreductase domain",
"short": "NADP_OxRdtase_dom"
},
"description": [
{
"text": "<p>The aldo-keto reductase family includes a number of related monomeric NADPH-dependent oxidoreductases, such as aldehyde reductase, aldose reductase, prostaglandin F synthase, xylose reductase, rho crystallin, and many others [[cite:PUB00002548]]. All possess a similar structure, with a β-α-β fold characteristic of nucleotide binding proteins [[cite:PUB00002605]]. The fold comprises a parallel β8/α8 barrel, which contains a novel NADP-binding motif. The binding site is located in a large, deep, elliptical pocket in the C-terminal end of the β-sheet, the substrate being bound in an extended conformation. The hydrophobic nature of the pocket favours aromatic and apolar substrates over highly polar ones [[cite:PUB00005156]].</p>\n\n<p>Binding of the NADPH coenzyme causes a massive conformational change, reorienting a loop, effectively locking the coenzyme in place. This binding is more similar to FAD- than to NAD(P)-binding oxidoreductases [[cite:PUB00002751]].</p>\n\n<p>Some proteins of this entry contain a K+ ion channel beta chain regulatory domain; these are reported to have oxidoreductase activity [[cite:PUB00015049]].</p>\n\n<p>This entry represents the NADP-dependent oxidoreductase domain found in these proteins.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00005156": {
"PMID": 1621098,
"ISBN": null,
"volume": "257",
"issue": "5066",
"year": 1992,
"title": "An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.",
"URL": null,
"raw_pages": "81-4",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Wilson DK",
"Bohren KM",
"Gabbay KH",
"Quiocho FA."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/257/5066/81"
},
"PUB00015049": {
"PMID": 10884227,
"ISBN": null,
"volume": "289",
"issue": "5476",
"year": 2000,
"title": "Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels.",
"URL": null,
"raw_pages": "123-7",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Gulbis JM",
"Zhou M",
"Mann S",
"MacKinnon R."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.289.5476.123"
},
"PUB00002605": {
"PMID": 2105951,
"ISBN": null,
"volume": "265",
"issue": "7",
"year": 1990,
"title": "Sequence analysis of bovine lens aldose reductase.",
"URL": null,
"raw_pages": "3628-35",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Schade SZ",
"Early SL",
"Williams TR",
"Kezdy FJ",
"Heinrikson RL",
"Grimshaw CE",
"Doughty CC."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/265/7/3628.pdf"
},
"PUB00002751": {
"PMID": 1447221,
"ISBN": null,
"volume": "267",
"issue": "34",
"year": 1992,
"title": "The crystal structure of the aldose reductase.NADPH binary complex.",
"URL": null,
"raw_pages": "24841-7",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Borhani DW",
"Harter TM",
"Petrash JM."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/267/34/24841"
},
"PUB00002548": {
"PMID": 2498333,
"ISBN": null,
"volume": "264",
"issue": "16",
"year": 1989,
"title": "The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.",
"URL": null,
"raw_pages": "9547-51",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Bohren KM",
"Bullock B",
"Wermuth B",
"Gabbay KH."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/264/16/9547.pdf"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036812",
"name": "NAD(P)-dependent oxidoreductase domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 1550,
"interactions": 0,
"matches": 309980,
"pathways": 122,
"proteins": 304687,
"proteomes": 20282,
"sets": 0,
"structural_models": {
"alphafold": 237490,
"bfvd": 9
},
"structures": 506,
"taxa": 38006
},
"entry_annotations": {
"alignment:seed": 26,
"alignment:full": 143305
},
"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": "GenProp1551",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1551"
},
{
"accession": "GenProp1263",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1263"
},
{
"accession": "GenProp1649",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1649"
},
{
"accession": "GenProp1552",
"url": "https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1552"
}
]
},
"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": "1.1.1",
"url": "https://enzyme.expasy.org/EC/1.1.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1pyf",
"name": "Structure of NADPH-dependent family 11 aldo-keto reductase AKR11A(apo)"
}
}
}
