{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"B6F209","uniProtkbId":"CPAS_ASPOZ","entryAudit":{"firstPublicDate":"2018-10-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-12-16","entryVersion":103,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Aspergillus oryzae","commonName":"Yellow koji mold","taxonId":5062,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Circumdati"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19663400"}],"value":"Cyclo-acetoacetyl-L-tryptophan synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19663400"}],"value":"2.3.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18854220"}],"value":"Cyclopiazonic acid biosynthesis cluster protein A"}},{"fullName":{"value":"Polyketide synthase-nonribosomal peptide synthetase cpaA"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18854220"}],"value":"PKS-NRPS cpaA"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18854220"}],"value":"cpaA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19663400"}],"value":"cpaS"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18854220"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19663400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19877600"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21608094"}],"value":"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the fungal neurotoxin cyclopiazonic acid (CPA), a nanomolar inhibitor of Ca(2+)-ATPase with a unique pentacyclic indole tetramic acid scaffold (PubMed:18854220, PubMed:19663400, PubMed:21608094). The hybrid two module polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) cpaS incorporates acetyl-CoA, malonyl-CoA, and tryptophan (Trp) and utilizes a C-terminal redox-incompetent reductase domain to make and release the tryptophan tetramic acid, cyclo-acetoacetyl-L-tryptophan (c-AATrp), as the first intermediate in the pathway. CpaS catalyzes a Dieckmann-type cyclization on the N-acetoacetyl-Trp intermediate bound in thioester linkage to the phosphopantetheinyl arm of the T domain to form and release c-AATrp (PubMed:18854220, PubMed:19663400, PubMed:21608094). CpaD then regiospecifically dimethylallylates c-AATrp to form beta-cyclopiazonic acid. CpaD discriminates against free Trp but accepts tryptophan-containing thiohydantoins, diketopiperazines, and linear peptides as substrates for C4-prenylation and also acts as regiospecific O-dimethylallyltransferase (DMAT) on a tyrosine-derived tetramic acid (PubMed:19877600). The beta-cyclopiazonate dehydrogenase cpaO then carries out the dehydrogenation of beta-CPA to yield an unstable enimine product, which is captured by intramolecular cyclization to create the pentacyclic fused scaffold of alpha-cyclopiazonate (PubMed:21608094). Finally, the cytochrome P450 monooxygenase cpaH mediates the conversion of CPA into the less toxic 2-oxocyclopiazonic acid, the end product of the CPA pathway in A.oryza (PubMed:21608094)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tryptophan + malonyl-CoA + acetyl-CoA = cyclo-acetoacetyl-L-tryptophan + CO2 + 2 CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66900"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:57912"},{"database":"ChEBI","id":"CHEBI:167552"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19663400"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66901"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19663400"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18854220"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19663400"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21608094"}],"value":"Secondary metabolite biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19663400"}],"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, epimerase (E) domains (responsible for L- to D- amino acid conversion) are present within the NRP synthetase. CpaA also contains a polyketide synthase module (PKS) consisting of several catalytic domains including a ketoacyl synthase domain (KS), an acyl transferase domain (AT), a dehydratase domain (DH), a methyltransferase domain (MT), and a ketoreductase domain (KR). Instead of a thioesterase domain (TE), CpaA finishes with a reductase-like domain (RED) for peptide release. CpaA has the following architecture: KS-AT-DH-KR-PCP-C-A-T-RED"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18854220"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21608094"}],"value":"Impairs the production of cyclopiazonic acid and of its biosynthetic intermediates cyclo-acetoacetyl-L-tryptophan and beta-cyclopiazonic acid"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the C-terminal section; belongs to the NRP synthetase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":3907,"modifier":"EXACT"}},"description":"Cyclo-acetoacetyl-L-tryptophan synthase","featureId":"PRO_0000445385"},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"Ketosynthase family 3 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ACTIVITY":1,"PATHWAY":1,"DOMAIN":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":4,"Region":10,"Active site":3,"Modified residue":2},"uniParcId":"UPI0001838201"}}