{"metadata":{"accession":"IPR001055","entry_id":null,"type":"family","go_terms":[{"identifier":"GO:0051537","name":"2 iron, 2 sulfur cluster binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0140647","name":"P450-containing electron transport chain","category":{"code":"P","name":"biological_process"}}],"source_database":"interpro","member_databases":{"panther":{"PTHR23426":"FERREDOXIN/ADRENODOXIN"},"prints":{"PR00355":"ADRENODOXIN"}},"integrated":null,"hierarchy":{"accession":"IPR001055","name":"Adrenodoxin-like","type":"Family","children":[{"accession":"IPR011536","name":"Ferredoxin 2Fe-2S type, proteobacteria","type":"Family","children":[]}]},"name":{"name":"Adrenodoxin-like","short":"Adrenodoxin-like"},"description":[{"text":"<p>Adrenodoxin, putidaredoxin, rhodocoxin and terpredoxin are soluble 2Fe-2S iron-sulphur proteins that act as single electron carriers. They are a subgroup of the ferredoxin family of iron-sulphur proteins.</p>\n\n<p>In mitochondrial monooxygenase systems, adrenodoxin transfers an electron from NADPH:adrenodoxin reductase to membrane-bound P450 [[cite:PUB00097471], [cite:PUB00016350]]. In bacteria, putidaredoxin and terpredoxin serve as electron carriers between corresponding NADH-dependent ferredoxin reductases and soluble P450 [[cite:PUB00002613], [cite:PUB00002723]]. The exact functions of other members of this family are not known.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00002613":{"PMID":2180940,"ISBN":null,"volume":"265","issue":"11","year":1990,"title":"Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins.","URL":null,"raw_pages":"6066-73","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Peterson JA","Lorence MC","Amarneh B."],"DOI_URL":"http://intl.jbc.org/cgi/content/abstract/265/11/6066"},"PUB00002723":{"PMID":1629218,"ISBN":null,"volume":"267","issue":"20","year":1992,"title":"Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon.","URL":null,"raw_pages":"14193-203","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Peterson JA","Lu JY","Geisselsoder J","Graham-Lorence S","Carmona C","Witney F","Lorence MC."],"DOI_URL":"http://intl.jbc.org/cgi/content/abstract/267/20/14193"},"PUB00016350":{"PMID":12069587,"ISBN":null,"volume":"41","issue":"25","year":2002,"title":"A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin.","URL":null,"raw_pages":"7969-78","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Beilke D","Weiss R","Lohr F","Pristovsek P","Hannemann F","Bernhardt R","Ruterjans H."],"DOI_URL":"http://dx.doi.org/10.1021/bi0160361"},"PUB00097471":{"PMID":22556163,"ISBN":null,"volume":"64","issue":"6","year":2012,"title":"Adrenodoxin--a versatile ferredoxin.","URL":null,"raw_pages":"506-12","medline_journal":"IUBMB Life","ISO_journal":"IUBMB Life","authors":["Ewen KM","Ringle M","Bernhardt R."],"DOI_URL":null}},"set_info":null,"overlaps_with":[{"accession":"IPR012675","name":"Beta-grasp domain superfamily","type":"homologous_superfamily"},{"accession":"IPR036010","name":"2Fe-2S ferredoxin-like superfamily","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":24713,"pathways":36,"proteins":24405,"proteomes":11775,"sets":0,"structural_models":{"alphafold":19504,"bfvd":0},"structures":68,"taxa":22841},"entry_annotations":{},"cross_references":{"prositedoc":{"displayName":"PROSITE Doc","description":"PROSITE is a database of protein families and domains.","rank":18,"accessions":[{"accession":"PDOC00642","url":"http://prosite.expasy.org/PDOC00642"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1ayf","name":"BOVINE ADRENODOXIN (OXIDIZED)"}}}