{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"I0J1I6","uniProtkbId":"BSR_PSETA","entryAudit":{"firstPublicDate":"2012-09-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2012-06-13","entryVersion":46,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Pseudomonas taetrolens","taxonId":47884,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19300994"}],"value":"Broad specificity amino-acid racemase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19300994"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20564572"}],"value":"5.1.1.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20564572"}],"value":"Arginine racemase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19300994"}],"value":"Broad substrate specificity racemase"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19300994"}],"value":"argR"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19300994"}],"value":"Amino-acid racemase able to utilize a broad range of substrates. 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The growth of the deletion mutant strain on LB medium is slightly retarded as compared to the wild type, which might indicate that ArgR is also generally involved in amino acid degradation"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the alanine racemase family. Bsr subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19300994"}]},{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Broad specificity amino-acid racemase","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"}],"featureId":"PRO_0000419111"},{"type":"Active site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"}]},{"type":"Active site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"}]},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"}]},{"type":"Disulfide bond","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_02212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20564572"}]},{"type":"Mutagenesis","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"The catalytic efficiency with arginine, lysine, and ornithine is very similar to that of wild-type, and that with both L-alanine and D-alanine increases approximately five times; when associated with A-96.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20564572"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"The catalytic efficiency with arginine, lysine, and ornithine is very similar to that of wild-type, and that with both L-alanine and D-alanine increases approximately five times; when associated with A-70.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20564572"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0574","category":"Cellular component","name":"Periplasm"},{"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"19300994","citationType":"journal article","authors":["Matsui D.","Oikawa T.","Arakawa N.","Osumi S.","Lausberg F.","Stabler N.","Freudl R.","Eggeling L."],"citationCrossReferences":[{"database":"PubMed","id":"19300994"},{"database":"DOI","id":"10.1007/s00253-009-1942-7"}],"title":"A periplasmic, pyridoxal-5'-phosphate-dependent amino acid racemase in Pseudomonas taetrolens.","publicationDate":"2009","journal":"Appl. 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