{"metadata":{"accession":"IPR051783","entry_id":null,"type":"family","go_terms":null,"source_database":"interpro","member_databases":{"panther":{"PTHR48079":"NAD(P)-dependent Metabolic Enzyme"}},"integrated":null,"hierarchy":{"accession":"IPR051783","name":"NAD(P)-dependent oxidoreductase-like","type":"Family","children":[{"accession":"IPR017829","name":"Hopanoid-associated sugar epimerase","type":"Family","children":[]}]},"name":{"name":"NAD(P)-dependent oxidoreductase-like","short":"NAD(P)-dependent_oxidoreduct"},"description":[{"text":"<p>This family of proteins includes enzymes that are involved in various metabolic processes, including the biosynthesis of sterols, antibiotics, and other bioactive molecules. Members of this family are characterised by their dependence on NAD(P) as a cofactor, performing functions such as oxidative decarboxylation, reduction, and dehydration reactions. These proteins are implicated in the modification of steroid molecules (NSDHL), the conversion of aurachins (AUAH) [[cite:PUB00154985]], and the biosynthesis of complex compounds like UCS1025A (UcsJ), which has antibacterial and antitumor properties [[cite:PUB00094509]]. The family also includes enzymes that participate in the conversion of antibiotics, such 2'-dehydrokanamycin reductase which converts 2'-dehydrokanamycin A into kanamycin A, contributing to their bioactivation [[cite:PUB00154984]]. The diverse enzymatic activities within this family reflect a broad functional repertoire, with each member playing a specific role in cellular metabolism and the biosynthesis of secondary metabolites.</p>","llm":true,"checked":true,"updated":true}],"wikipedia":null,"literature":{"PUB00154984":{"PMID":22374809,"ISBN":null,"volume":"51","issue":"14","year":2012,"title":"The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the α-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK.","URL":null,"raw_pages":"3428-31","medline_journal":"Angew Chem Int Ed Engl","ISO_journal":"Angew Chem Int Ed Engl","authors":["Sucipto H","Kudo F","Eguchi T."],"DOI_URL":"https://doi.org/10.1002/anie.201108122"},"PUB00094509":{"PMID":29373009,"ISBN":null,"volume":"140","issue":"6","year":2018,"title":"Genome Mining and Assembly-Line Biosynthesis of the UCS1025A Pyrrolizidinone Family of Fungal Alkaloids.","URL":null,"raw_pages":"2067-2071","medline_journal":"J Am Chem Soc","ISO_journal":"J. Am. Chem. Soc.","authors":["Li L","Tang MC","Tang S","Gao S","Soliman S","Hang L","Xu W","Ye T","Watanabe K","Tang Y."],"DOI_URL":null},"PUB00154985":{"PMID":22907798,"ISBN":null,"volume":"51","issue":"37","year":2012,"title":"A semipinacol rearrangement directed by an enzymatic system featuring dual-function FAD-dependent monooxygenase.","URL":null,"raw_pages":"9437-40","medline_journal":"Angew Chem Int Ed Engl","ISO_journal":"Angew Chem Int Ed Engl","authors":["Katsuyama Y","Harmrolfs K","Pistorius D","Li Y","Muller R."],"DOI_URL":"https://doi.org/10.1002/anie.201204138"}},"set_info":null,"overlaps_with":[{"accession":"IPR036291","name":"NAD(P)-binding domain superfamily","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":54495,"pathways":0,"proteins":54495,"proteomes":14285,"sets":0,"structural_models":{"alphafold":40638,"bfvd":0},"structures":3,"taxa":24781},"entry_annotations":{},"cross_references":{},"is_llm":true,"is_reviewed_llm":true,"is_updated_llm":true,"representative_structure":{"accession":"3gpi","name":"Structure of putative NAD-dependent epimerase/dehydratase from methylobacillus flagellatus"}}}