{"metadata":{"accession":"PF01958","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR002811","hierarchy":null,"name":{"name":"Aspartate dehydrogenase, C-terminal","short":"Asp_DH_C"},"description":[{"text":"<p>This entry represents the C-terminal domain of aspartate dehydrogenases that belong to a unique class of amino acid dehydrogenases. The structure of Thermotoga maritima TM1643 has been found to contain an N-terminal Rossmann fold domain (which binds the NAD(P)+ cofactor) and a C-terminal alpha/beta domain [[cite:PUB00014412]]. Enzymatic characterisation of TM1643 revealed that it possesses NAD or NADP-dependent dehydrogenase activity toward L-aspartate but no aspartate oxidase activity [[cite:PUB00014412]]. Members of this group share some structural similarity to several other NAD(P)+-dependent oxidoreductases, including inositol 1-phosphate synthase, dihydrodipicolinate reductase, and ASA-DH [[cite:PUB00014412]]. It has been proposed that in Thermotoga maritima, TM1643 catalyses the first reaction of de novo biosynthesis of NAD from aspartate, and it produces iminoaspartate required for this pathway.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00014412":{"PMID":12496312,"ISBN":null,"volume":"278","issue":"10","year":2003,"title":"Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643.","URL":null,"raw_pages":"8804-8","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Yang Z","Savchenko A","Yakunin A","Zhang R","Edwards A","Arrowsmith C","Tong L."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M211892200"}},"set_info":{"accession":"CL0139","name":"GADPH_aa-bio_dh"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":31,"interactions":0,"matches":3195,"pathways":0,"proteins":3184,"proteomes":2698,"sets":1,"structural_models":{"alphafold":2258},"structures":3,"taxa":5585},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":83,"alignment:full":1753},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}