{"metadata":{"accession":"PF01941","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR027790","hierarchy":null,"name":{"name":"S-adenosylmethionine synthetase (AdoMet synthetase)","short":"AdoMet_Synthase"},"description":[{"text":"<p>This family consists of several archaebacterial S-adenosylmethionine synthetase C(AdoMet synthetase or MAT) (EC 2.5.1.6). S-Adenosylmethionine (AdoMet) occupies a central role in the metabolism of all cells. The biological roles of AdoMet include acting as the primary methyl group donor, as a precursor to the polyamines, and as a progenitor of a 5'-deoxyadenosyl radical. S-Adenosylmethionine synthetase catalyses the only known route of AdoMet biosynthesis. The synthetic process occurs in a unique reaction in which the complete triphosphate chain is displaced from ATP and a sulfonium ion formed. MATs from various organisms contain ~400-amino acid polypeptide chains [[cite:PUB00019110]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00019110":{"PMID":11872742,"ISBN":null,"volume":"277","issue":"19","year":2002,"title":"Enzymatic properties of S-adenosylmethionine synthetase from the archaeon Methanococcus jannaschii.","URL":null,"raw_pages":"16624-31","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Lu ZJ","Markham GD."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M110456200"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":3,"interactions":0,"matches":991,"pathways":0,"proteins":974,"proteomes":897,"sets":0,"structural_models":{"alphafold":794},"structures":12,"taxa":1739},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":73,"alignment:full":477},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"6s81","name":"Crystal structure of methionine adenosyltransferase from Pyrococcus furiosus"}}}