HTTP 200 OK
Allow: GET, HEAD
Cached: true
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Server-Timing:
Vary: Accept
{
"metadata": {
"accession": "IPR012999",
"entry_id": null,
"type": "active_site",
"go_terms": [
{
"identifier": "GO:0016668",
"name": "oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"prosite": {
"PS00076": "Pyridine nucleotide-disulphide oxidoreductases class-I active site"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR012999",
"name": "Pyridine nucleotide-disulphide oxidoreductase, class I, active site",
"type": "Active_site",
"children": []
},
"name": {
"name": "Pyridine nucleotide-disulphide oxidoreductase, class I, active site",
"short": "Pyr_OxRdtase_I_AS"
},
"description": [
{
"text": "<p>The pyridine nucleotide-disulphide oxidoreductases are FAD flavoproteins which contain a pair of redox-active cysteines involved in the transfer of reducing equivalents from the FAD cofactor to the substrate. On the basis of sequence and structural similarities [[cite:PUB00004100]] these enzymes can be classified into two categories. The first category groups together the following enzymes [[cite:PUB00003204], [cite:PUB00000149], [cite:PUB00005377], [cite:PUB00001694]]:</p>\r\n\r\n<ul>\r\n<li>Glutathione reductase ([ec:1.8.1.7]) (GR).</li>\r\n<li>Higher eukaryotes thioredoxin reductase ([ec:1.8.1.9]).</li>\r\n<li>Trypanothione reductase ([ec:1.8.1.12]).</li>\r\n<li>Lipoamide dehydrogenase ([ec:1.8.1.4]), the E3 component of alpha-ketoacid dehydrogenase complexes.</li>\r\n<li>Mercuric reductase ([ec:1.16.1.1]).</li>\r\n</ul>\r\n \r\n<p>The sequence around the two cysteines involved in the redox-active disulphide bond is conserved and can be used as a signature pattern.</p>\r\n\r\n<p>Note: In positions 6 and 7 of the pattern all known sequences have Asn-(Val/ Ile) with the exception of GR from plant chloroplasts and from cyanobacteria which have Ile-Arg [[cite:PUB00004526]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00004100": {
"PMID": 2067578,
"ISBN": null,
"volume": "352",
"issue": "6331",
"year": 1991,
"title": "Convergent evolution of similar function in two structurally divergent enzymes.",
"URL": null,
"raw_pages": "172-4",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Kuriyan J",
"Krishna TS",
"Wong L",
"Guenther B",
"Pahler A",
"Williams CH Jr",
"Model P."
],
"DOI_URL": "http://dx.doi.org/10.1038/352172a0"
},
"PUB00003204": {
"PMID": 6546954,
"ISBN": null,
"volume": "174",
"issue": "3",
"year": 1984,
"title": "Structural relationship between glutathione reductase and lipoamide dehydrogenase.",
"URL": null,
"raw_pages": "483-96",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Rice DW",
"Schulz GE",
"Guest JR."
],
"DOI_URL": "http://dx.doi.org/10.1016/0022-2836(84)90332-2"
},
"PUB00000149": {
"PMID": 2643922,
"ISBN": null,
"volume": "268",
"issue": "2",
"year": 1989,
"title": "Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases.",
"URL": null,
"raw_pages": "409-25",
"medline_journal": "Arch Biochem Biophys",
"ISO_journal": "Arch. Biochem. Biophys.",
"authors": [
"Carothers DJ",
"Pons G",
"Patel MS."
],
"DOI_URL": "http://dx.doi.org/10.1016/0003-9861(89)90309-3"
},
"PUB00005377": {
"PMID": 1957352,
"ISBN": null,
"volume": "16",
"issue": "8",
"year": 1991,
"title": "Molecular studies on trypanothione reductase, a target for antiparasitic drugs.",
"URL": null,
"raw_pages": "305-9",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Walsh C",
"Bradley M",
"Nadeau K."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(91)90124-E"
},
"PUB00001694": {
"PMID": 7589432,
"ISBN": null,
"volume": "373",
"issue": "1",
"year": 1995,
"title": "Cloning and sequencing of a human thioredoxin reductase.",
"URL": null,
"raw_pages": "5-9",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Gasdaska PY",
"Gasdaska JR",
"Cochran S",
"Powis G."
],
"DOI_URL": "http://dx.doi.org/10.1016/0014-5793(95)01003-W"
},
"PUB00004526": {
"PMID": 1303792,
"ISBN": null,
"volume": "2",
"issue": "1",
"year": 1992,
"title": "Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.).",
"URL": null,
"raw_pages": "129-31",
"medline_journal": "Plant J",
"ISO_journal": "Plant J.",
"authors": [
"Creissen G",
"Edwards EA",
"Enard C",
"Wellburn A",
"Mullineaux P."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 79053,
"pathways": 102,
"proteins": 79044,
"proteomes": 20050,
"sets": 0,
"structural_models": {
"alphafold": 62796,
"bfvd": 0
},
"structures": 258,
"taxa": 36710
},
"entry_annotations": {},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00073",
"url": "http://prosite.expasy.org/PDOC00073"
}
]
},
"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": "1.8.1",
"url": "https://enzyme.expasy.org/EC/1.8.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
