{"metadata":{"accession":"IPR046952","entry_id":null,"type":"family","go_terms":[{"identifier":"GO:0050660","name":"flavin adenine dinucleotide binding","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0045454","name":"cell redox homeostasis","category":{"code":"P","name":"biological_process"}}],"source_database":"interpro","member_databases":{"panther":{"PTHR42737":"GLUTATHIONE REDUCTASE"}},"integrated":null,"hierarchy":{"accession":"IPR001100","name":"Pyridine nucleotide-disulphide oxidoreductase, class I","type":"Family","children":[{"accession":"IPR006258","name":"Dihydrolipoamide dehydrogenase","type":"Family","children":[]},{"accession":"IPR017817","name":"Mycothione reductase","type":"Family","children":[]},{"accession":"IPR021179","name":"Mercury(II) reductase","type":"Family","children":[]},{"accession":"IPR022962","name":"Soluble pyridine nucleotide transhydrogenase, gammaproteobacteria","type":"Family","children":[]},{"accession":"IPR046952","name":"Glutathione reductase/thioredoxin reductase-like","type":"Family","children":[{"accession":"IPR001864","name":"Trypanothione reductase","type":"Family","children":[]},{"accession":"IPR006322","name":"Glutathione reductase, eukaryote/bacterial","type":"Family","children":[]},{"accession":"IPR006324","name":"Glutathione reductase","type":"Family","children":[]},{"accession":"IPR006338","name":"Thioredoxin/glutathione reductase selenoprotein","type":"Family","children":[]}]}]},"name":{"name":"Glutathione reductase/thioredoxin reductase-like","short":"GSHR/TRXR-like"},"description":[{"text":"<p>There are two major pathways for regulating cellular redox homeostasis, antioxidant defense and to provide reducing equivalents for a variety of chemical transformations in most organisms, which involve glutathione/glutathione disulfide (GSH/GSSG) and the thioredoxin (Trx) dependent systems. They include GSSG reductase (GR) for recycling oxidized glutathione using NADPH , while Trx system includes a NADPH dependent reductase Trx reductase (TrxR). GR and TrxR are closely related oxidoreductases with highly similar structure and reaction mechanism, belonging to the GR superfamily of dimeric flavoenzymes [[cite:PUB00101438]]. This family also includes trypanothione reductase, a closely related which also belongs to GR superfamily.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00101438":{"PMID":21782895,"ISBN":null,"volume":"1810","issue":"12","year":2011,"title":"Thioredoxin glutathione reductase: its role in redox biology and potential as a target for drugs against neglected diseases.","URL":null,"raw_pages":"1262-71","medline_journal":"Biochim Biophys Acta","ISO_journal":"Biochim Biophys Acta","authors":["Prast-Nielsen S","Huang HH","Williams DL."],"DOI_URL":null}},"set_info":null,"overlaps_with":[{"accession":"IPR036188","name":"FAD/NAD(P)-binding domain superfamily","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":23719,"pathways":38,"proteins":23719,"proteomes":9391,"sets":0,"structural_models":{"alphafold":20325,"bfvd":0},"structures":192,"taxa":21311},"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":"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":{"accession":"1k4q","name":"Human Glutathione Reductase Inactivated by Peroxynitrite"}}}