{"id":"b654120c-2e3c-5f00-b5b1-1f46f9c05c9f","stable_key":"59b18080-c560-563d-abc5-bac4ee82a27c:ergothioneine-egtc-amide","predicate":"processes","statement":"Mycobacterium smegmatis EgtC removes the glutamyl portion of the ergothioneine-pathway sulfur adduct.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"41215179-a4fd-5f74-9768-f59b67544740","mechanism_event_label":"A separate enzyme removes the carrier part of the sulfur donor.","subject":{"id":"e3f28f4d-98f7-5efd-a05e-2a9735cb47cf","slug":"mycobacterium-smegmatis-egtc","display_name":"Mycobacterium smegmatis EgtC","entity_type_key":"protein"},"object":{"id":"8a0617df-cacc-55b1-b5ff-3b28afa12f20","slug":"hercynyl-gamma-glutamylcysteine-sulfoxide","display_name":"Hercynyl-gamma-glutamylcysteine sulfoxide","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"41215179-a4fd-5f74-9768-f59b67544740","stable_key":"59b18080-c560-563d-abc5-bac4ee82a27c:ergothioneine-egtc-amide-event","event_type":"observed_relationship","label":"A separate enzyme removes the carrier part of the sulfur donor.","description":"Mycobacterium smegmatis EgtC removes the glutamyl portion of the ergothioneine-pathway sulfur adduct.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"e3f28f4d-98f7-5efd-a05e-2a9735cb47cf","slug":"mycobacterium-smegmatis-egtc","display_name":"Mycobacterium smegmatis EgtC","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"8a0617df-cacc-55b1-b5ff-3b28afa12f20","slug":"hercynyl-gamma-glutamylcysteine-sulfoxide","display_name":"Hercynyl-gamma-glutamylcysteine sulfoxide","entity_type_key":"small_molecule"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"939c92c3-50ea-5a4a-9654-8e3b94448132","slug":"ergothioneine","display_name":"L-Ergothioneine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"f7086495-5e10-536b-81b3-e63590cf156d","slug":"hercynylcysteine-sulfoxide","display_name":"Hercynylcysteine sulfoxide","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Substrate-bound bacterial EgtC structure.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Not human glutathione breakdown; EgtC homologs can have other functions.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Ergothioneine collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"ergothioneine","display_name":"L-Ergothioneine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"A separate enzyme removes the carrier part of the sulfur donor.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Structure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26079795/ · DOI 10.1002/cbic.201500168","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"89a4a395-bf70-52d9-80cf-ec4e97d4c3a9","evidence_kind":"source_excerpt","locator":"Lines 192-198","start_line":192,"end_line":198,"excerpt":"## ergothioneine-egtc-amide\nA separate enzyme removes the carrier part of the sulfur donor.\nMycobacterium smegmatis EgtC removes the glutamyl portion of the ergothioneine-pathway sulfur adduct.\nModel: Substrate-bound bacterial EgtC structure.\nLimitations: Not human glutathione breakdown; EgtC homologs can have other functions.\nEvidence access: Primary abstract\nStructure of the Ergothioneine-Biosynthesis Amidohydrolase EgtC. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26079795/ · DOI 10.1002/cbic.201500168","model_system":"Substrate-bound bacterial EgtC structure.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"2f037d98-f3d0-5dbe-80d8-90b738f130d6","stable_key":"import-59b18080-c560-563d-abc5-bac4ee82a27c","title":"Ergothioneine: transport, redox chemistry and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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