{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q00869","uniProtkbId":"ESYN_FUSEQ","entryAudit":{"firstPublicDate":"2002-11-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-10-01","entryVersion":121,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Fusarium equiseti","commonName":"Fusarium scirpi","taxonId":61235,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Nectriaceae","Fusarium","Fusarium incarnatum-equiseti species complex"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8483420"}],"value":"Enniatin synthase"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7601090"}],"value":"Nonribosomal cyclopeptide synthetase ESYN1"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7601090"}],"value":"N-methylcyclopeptide synthetase"},"ecNumbers":[{"value":"6.3.2.-"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7601090"}],"value":"S-adenosyl-L-methionine-dependent N-methyltransferase"},"ecNumbers":[{"value":"2.1.1.-"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"7601090"}],"value":"ESYN1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10887181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7601090"}],"value":"Nonribosomal peptide synthetase that synthesizes enniatin by coupling three D-hydroxycarboxylic acids and three L-amino acids via amide and ester bonds in an alternating fashion (PubMed:10887181, PubMed:7601090). Whereas ESYN1 can accept different amino acids as precursors (L -valine, L-isoleucine or L-leucine), only one species of D-hydroxycarboxylic acid can be found in natural enniatin isolates (D-hydroxyisovaleric acid, D-Hiv) (PubMed:10887181, PubMed:7601090). D-Hiv stems from L-valine deanimation by a valine aminotransferase to 2-keto-isovaleric acid (2-Kiv), which becomes subsequently reduced by a keto-isovaleric acid reductase (KivR) to D-Hiv (PubMed:10887181, PubMed:7601090). Peptide bond formation and N-methylation of the amino acid occur before three enzyme-bound dipeptidols are condensed to a hexapeptidol (PubMed:10887181, PubMed:7601090)"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"pantetheine 4'-phosphate","evidences":[{"evidenceCode":"ECO:0000305"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:47942"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Binds 6 phosphopantetheines covalently."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"The N-methylation activity is inhibited by S-adenosyl-L-homocysteine and sinefugin"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10887181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7601090"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8483420"}],"value":"Antibiotic biosynthesis; enniatin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10887181"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"8483420"}],"value":"NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, additional domains required for further modifications are also present (Probable). Enniatin synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (Probable). The precursors D-hydroxycarboxylic acids and L-amino acids become activated at the A1 and the A2 domains. N-methylation of the amino acid takes place at the MT-domain. The building blocks are transferred from one module to another by means of T-domains and are ultimately stored at the waiting position T2b. Condensation of the building blocks and final cyclization and release from the enzyme is catalyzed by the C-domains (Probable)"}],"commentType":"DOMAIN"},{"texts":[{"value":"The N-terminus is blocked"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15707993"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16562855"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17326668"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9170286"}],"value":"Enniatins have antimicrobial, antiviral and cytotoxic properties (PubMed:16562855, PubMed:17326668, PubMed:9170286). The bioactivity of enniatins can be linked to their inhibition of drug efflux pumps (PubMed:15707993)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ATP-dependent AMP-binding enzyme family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":3131,"modifier":"EXACT"}},"description":"Enniatin synthase","featureId":"PRO_0000180306"},{"type":"Domain","location":{"start":{"value":1010,"modifier":"EXACT"},"end":{"value":1086,"modifier":"EXACT"}},"description":"Carrier 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}]},{"type":"Domain","location":{"start":{"value":2504,"modifier":"EXACT"},"end":{"value":2578,"modifier":"EXACT"}},"description":"Carrier 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