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{
"metadata": {
"accession": "IPR012748",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0008942",
"name": "nitrite reductase [NAD(P)H] activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd03529": "Rieske_NirD"
},
"pfam": {
"PF13806": "Rieske-like [2Fe-2S] domain"
},
"ncbifam": {
"TIGR02378": "nitrite reductase small subunit NirD"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR012748",
"name": "Rieske-like [2Fe-2S] domain, NirD-type",
"type": "Domain",
"children": []
},
"name": {
"name": "Rieske-like [2Fe-2S] domain, NirD-type",
"short": "Rieske-like_NirD"
},
"description": [
{
"text": "<p>In Proteobacteria and Actinobacteria the main nitrite reductase activity is contributed by the NADH-dependent nitrite reductase, which detoxifies the nitrite formed as the product of nitrate reduction. The NADH-nitrite reductase operon consists of 4 genes: nirB, nirD, nirC and cysG. The enzyme is formed by the two subunits nirB and nirD. NirC is a nitrite transporter and cysG is required for the synthesis of sirohaem, a cofactor of the nirB subunit [[cite:PUB00043673], [cite:PUB00043674]]. NirD displays some sequence similarities with the 2Fe-2S Rieske domain (see [prositedoc:PDOC00177]), but it does not contain the essential residues for the coordination of the iron sulphur [[cite:PUB00080966], [cite:PUB00043837]].</p>\r\n\r\n<p>The entry includes the NirD subunit. Members include bacterial and fungal proteins. The bacterial NirD contains a single Rieske domain while fungal proteins have a C-terminal Rieske domain in addition to several other domains. The fungal NirD is involved in nutrient acquisition, functioning at the soil/fungus interface to control nutrient exchange between the fungus and the host plant [[cite:PUB00080961], [cite:PUB00014871]]. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The Rieske [2Fe-2S] cluster is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs [[cite:PUB00043836]]. In this family, only a few members contain these residues. Other members may have lost the ability to bind the Rieske [2Fe-2S] cluster.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00043837": {
"PMID": 16271700,
"ISBN": null,
"volume": "1710",
"issue": "1",
"year": 2005,
"title": "Multiple Rieske proteins in prokaryotes: where and why?",
"URL": null,
"raw_pages": "1-12",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Schneider D",
"Schmidt CL."
],
"DOI_URL": null
},
"PUB00043836": {
"PMID": 16168954,
"ISBN": null,
"volume": "338",
"issue": "1",
"year": 2005,
"title": "Rieske business: structure-function of Rieske non-heme oxygenases.",
"URL": null,
"raw_pages": "175-90",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem. Biophys. Res. Commun.",
"authors": [
"Ferraro DJ",
"Gakhar L",
"Ramaswamy S."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.bbrc.2005.08.222"
},
"PUB00080966": {
"PMID": 11460929,
"ISBN": null,
"volume": "33",
"issue": "1",
"year": 2001,
"title": "A comprehensive phylogenetic analysis of Rieske and Rieske-type iron-sulfur proteins.",
"URL": null,
"raw_pages": "9-26",
"medline_journal": "J Bioenerg Biomembr",
"ISO_journal": "J. Bioenerg. Biomembr.",
"authors": [
"Schmidt CL",
"Shaw L."
],
"DOI_URL": "http://dx.doi.org/10.1023/A:1005616505962"
},
"PUB00043674": {
"PMID": 2200672,
"ISBN": null,
"volume": "191",
"issue": "2",
"year": 1990,
"title": "Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome.",
"URL": null,
"raw_pages": "315-23",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Peakman T",
"Crouzet J",
"Mayaux JF",
"Busby S",
"Mohan S",
"Harborne N",
"Wootton J",
"Nicolson R",
"Cole J."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1990.tb19125.x"
},
"PUB00080961": {
"PMID": 8694757,
"ISBN": null,
"volume": "317 ( Pt 1)",
"issue": null,
"year": 1996,
"title": "Purification and characterization of assimilatory nitrite reductase from Candida utilis.",
"URL": null,
"raw_pages": "147-55",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Sengupta S",
"Shaila MS",
"Rao GR."
],
"DOI_URL": "http://dx.doi.org/10.1042/bj3170147"
},
"PUB00043673": {
"PMID": 8919448,
"ISBN": null,
"volume": "136",
"issue": "1",
"year": 1996,
"title": "Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation?",
"URL": null,
"raw_pages": "1-11",
"medline_journal": "FEMS Microbiol Lett",
"ISO_journal": "FEMS Microbiol. Lett.",
"authors": [
"Cole J."
],
"DOI_URL": "http://dx.doi.org/10.1016/0378-1097(95)00480-7"
},
"PUB00014871": {
"PMID": 12665993,
"ISBN": null,
"volume": "43",
"issue": "3",
"year": 2003,
"title": "Characterisation and expression analysis of a nitrate transporter and nitrite reductase genes, two members of a gene cluster for nitrate assimilation from the symbiotic basidiomycete Hebeloma cylindrosporum.",
"URL": null,
"raw_pages": "199-205",
"medline_journal": "Curr Genet",
"ISO_journal": "Curr. Genet.",
"authors": [
"Jargeat P",
"Rekangalt D",
"Verner MC",
"Gay G",
"Debaud JC",
"Marmeisse R",
"Fraissinet-Tachet L."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036922",
"name": "Rieske [2Fe-2S] iron-sulphur domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 61,
"interactions": 0,
"matches": 14419,
"pathways": 0,
"proteins": 14407,
"proteomes": 9338,
"sets": 0,
"structural_models": {
"alphafold": 10440,
"bfvd": 0
},
"structures": 4,
"taxa": 15438
},
"entry_annotations": {
"alignment:seed": 31,
"alignment:full": 4200
},
"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": "1.7.1",
"url": "https://enzyme.expasy.org/EC/1.7.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "4aiv",
"name": "Crystal Structure of putative NADH-dependent nitrite reductase small subunit from Mycobacterium tuberculosis"
}
}
}
