{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A1DN09","uniProtkbId":"ANAPS_ASPF1","entryAudit":{"firstPublicDate":"2016-11-30","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-01-23","entryVersion":106,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Aspergillus fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181)","commonName":"Neosartorya fischeri","taxonId":331117,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Fumigati"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19001367"}],"value":"Nonribosomal peptide synthetase anaPS"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20225828"}],"value":"6.3.2.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19001367"}],"value":"Acetylaszonalenin synthesis protein anaPS"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19001367"}],"value":"anaPS"},"orfNames":[{"value":"NFIA_055290"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19001367"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20225828"}],"value":"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the prenylated pyrroloindoline diketopiperazine acetylaszonalenin (PubMed:19001367). The first step in the pathway is the formation of (R)-benzodiazepinedione by condensation of tryptophan and anthranilic acid catalyzed by the non-ribosomal peptide synthetase anaPS (PubMed:19001367, PubMed:20225828). The prenyltransferase anaPT then converts (R)-benzodiazepinedione to aszonalenin in the presence of dimethylallyl diphosphate (DMAPP) via C3-prenylation (PubMed:19001367). The last step in the biosynthesis of acetylaszonalenin via acetylation of aszonalenin at position N1 catalyzed by anaAT (PubMed:19001367)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"anthranilate + L-tryptophan + 2 ATP = (R)-benzodiazepinedione + 2 AMP + 2 diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:73003"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16567"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57912"},{"database":"ChEBI","id":"CHEBI:188914"},{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20225828"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:73004"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20225828"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19001367"}],"value":"Alkaloid biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19001367"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20225828"}],"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. NRPS12 has the following architecture: A-T-C-A-T-C (PubMed:19001367, PubMed:20225828). The activation and loading of antranilate is performed by the first module (PubMed:20225828)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the NRP synthetase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":2359,"modifier":"EXACT"}},"description":"Nonribosomal peptide synthetase anaPS","featureId":"PRO_0000438416"},{"type":"Domain","location":{"start":{"value":770,"modifier":"EXACT"},"end":{"value":846,"modifier":"EXACT"}},"description":"Carrier 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}]},{"type":"Domain","location":{"start":{"value":1842,"modifier":"EXACT"},"end":{"value":1918,"modifier":"EXACT"}},"description":"Carrier 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}]},{"type":"Region","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":633,"modifier":"EXACT"}},"description":"Adenylation 1","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":883,"modifier":"EXACT"},"end":{"value":1292,"modifier":"EXACT"}},"description":"Condensation 1","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":1321,"modifier":"EXACT"},"end":{"value":1709,"modifier":"EXACT"}},"description":"Adenylation 2","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":1936,"modifier":"EXACT"},"end":{"value":2356,"modifier":"EXACT"}},"description":"Condensation 2","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Modified residue","location":{"start":{"value":807,"modifier":"EXACT"},"end":{"value":807,"modifier":"EXACT"}},"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}]},{"type":"Modified residue","location":{"start":{"value":1879,"modifier":"EXACT"},"end":{"value":1879,"modifier":"EXACT"}},"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00258"}]}],"keywords":[{"id":"KW-0017","category":"Biological process","name":"Alkaloid metabolism"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0596","category":"PTM","name":"Phosphopantetheine"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"18404212","citationType":"journal article","authors":["Fedorova N.D.","Khaldi N.","Joardar V.S.","Maiti R.","Amedeo P.","Anderson M.J.","Crabtree J.","Silva J.C.","Badger J.H.","Albarraq A.","Angiuoli S.","Bussey H.","Bowyer P.","Cotty P.J.","Dyer P.S.","Egan A.","Galens K.","Fraser-Liggett C.M.","Haas B.J.","Inman J.M.","Kent R.","Lemieux S.","Malavazi I.","Orvis J.","Roemer T.","Ronning C.M.","Sundaram J.P.","Sutton G.","Turner G.","Venter J.C.","White O.R.","Whitty B.R.","Youngman P.","Wolfe K.H.","Goldman G.H.","Wortman J.R.","Jiang B.","Denning D.W.","Nierman W.C."],"citationCrossReferences":[{"database":"PubMed","id":"18404212"},{"database":"DOI","id":"10.1371/journal.pgen.1000046"}],"title":"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus.","publicationDate":"2008","journal":"PLoS Genet.","firstPage":"E1000046","lastPage":"E1000046","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"19001367","citationType":"journal article","authors":["Yin W.B.","Grundmann A.","Cheng J.","Li S.M."],"citationCrossReferences":[{"database":"PubMed","id":"19001367"},{"database":"DOI","id":"10.1074/jbc.m807606200"}],"title":"Acetylaszonalenin biosynthesis in Neosartorya fischeri. Identification of the biosynthetic gene cluster by genomic mining and functional proof of the genes by biochemical investigation.","publicationDate":"2009","journal":"J. Biol. 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