{"metadata":{"accession":"PF20906","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR048350","hierarchy":null,"name":{"name":"S-Me-THD-like, C-terminal domain","short":"S-Me-THD_C"},"description":[{"text":"<p>This beta barrel domain is found at the C-terminal of S-methyl thiohydantoin desulfurase from Variovorax sp. (S-Me-THD) and similar sequences mainly found in bacteria and fungi. S-Me-THD catalyses the hydrolysis of S-methyl -thiohydantoin-5-propanoate into hydantoin-5-propanoate and methanethiol, the third step in S-methyl ergothioneine degradation [[cite:PUB00155448]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00155448":{"PMID":38389448,"ISBN":null,"volume":"19","issue":"3","year":2024,"title":"Structure and Substrate Specificity of <i>S</i>-Methyl Thiourocanate Hydratase.","URL":null,"raw_pages":"718-724","medline_journal":"ACS Chem Biol","ISO_journal":"ACS Chem Biol","authors":["Vasseur CM","Karunasegaram D","Seebeck FP."],"DOI_URL":"https://doi.org/10.1021/acschembio.3c00745"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":53,"interactions":0,"matches":4979,"pathways":0,"proteins":4960,"proteomes":2804,"sets":0,"structural_models":{"alphafold":3385},"structures":1,"taxa":5281},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":145,"alignment:full":2924},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}