{"metadata":{"accession":"PF02679","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR003830","hierarchy":null,"name":{"name":"(2R)-phospho-3-sulfolactate synthase (ComA)","short":"ComA"},"description":[{"text":"<p>In methanobacteria (2R)-phospho-3-sulfolactate synthase (ComA) catalyses the first step of the biosynthesis of coenzyme M from phosphoenolpyruvate (P-enolpyruvate). This novel enzyme catalyses the stereospecific Michael addition of sulfite to P-enolpyruvate, forming L-2-phospho-3-sulfolactate (PSL). It is suggested that the ComA-catalysed reaction is analogous to those reactions catalysed by beta-elimination enzymes that proceed through an enolate intermediate [[cite:PUB00010730]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00010730":{"PMID":11830598,"ISBN":null,"volume":"277","issue":"16","year":2002,"title":"Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes.","URL":null,"raw_pages":"13421-9","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Graham DE","Xu H","White RH."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M201011200"}},"set_info":{"accession":"CL0036","name":"TIM_barrel"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":37,"interactions":0,"matches":2796,"pathways":0,"proteins":2768,"proteomes":2472,"sets":1,"structural_models":{"alphafold":2010},"structures":3,"taxa":4674},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":88,"alignment:full":1726},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"1qwg","name":"Crystal structure of Methanococcus jannaschii phosphosulfolactate synthase"}}}