{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"I0DFJ0","secondaryAccessions":["A0A080UMP9"],"uniProtkbId":"AADC_BACAT","entryAudit":{"firstPublicDate":"2023-02-22","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2012-06-13","entryVersion":55,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bacillus atrophaeus","taxonId":1452,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Bacillaceae","Bacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"23628927"}],"value":"Aromatic-L-amino-acid decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"23628927"}],"value":"AADC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23628927"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33713143"}],"value":"4.1.1.28"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"33713143"}],"value":"AADC-BA"}}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23628927"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33713143"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23628927"}],"value":"Involved in bacillamide C biosynthesis (Probable). Catalyzes the decarboxylation of L-tryptophan to tryptamine (PubMed:23628927, PubMed:33713143). The tryptamine obtained is then probably incorporated into the bacillamide C peptide, which is derived from the amino acids alanine, cysteine and tryptophan through nonribosomal peptide synthetase (NRPS) biosynthesis strategy (Probable). L-tryptophan is the best substrate, but the enzyme displays broad substrate specificity for various aromatic amino acids in vitro and it can also catalyze the decarboxylation of L-phenylalanine, 5-hydroxy-L-tryptophan (L-HTP) and L-DOPA, with lower efficiency (PubMed:23628927, PubMed:33713143). 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Loses most of its activity above 55 degrees Celsius (PubMed:33713143)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33713143"}],"value":"The broad substrate specificity of AADC-BA could be exploited to produce various aromatic biogenic amines"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the group II decarboxylase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"Aromatic-L-amino-acid decarboxylase","featureId":"PRO_0000457344"},{"type":"Modified residue","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"A7B1V0"}]}],"keywords":[{"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"}],"references":[{"referenceNumber":1,"citation":{"id":"23628927","citationType":"journal article","authors":["Yuwen L.","Zhang F.L.","Chen Q.H.","Lin S.J.","Zhao Y.L.","Li Z.Y."],"citationCrossReferences":[{"database":"PubMed","id":"23628927"},{"database":"DOI","id":"10.1038/srep01753"}],"title":"The role of aromatic L-amino acid decarboxylase in bacillamide C biosynthesis by Bacillus atrophaeus C89.","publicationDate":"2013","journal":"Sci. 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