{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P10724","uniProtkbId":"ALR_GEOSE","entryAudit":{"firstPublicDate":"1989-07-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1997-11-01","entryVersion":155,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Geobacillus stearothermophilus","commonName":"Bacillus stearothermophilus","taxonId":1422,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Anoxybacillaceae","Geobacillus"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Alanine racemase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10079072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12203980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12741835"}],"value":"5.1.1.1"}]}},"genes":[{"geneName":{"value":"alr"},"synonyms":[{"value":"dal"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10502689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12203980"}],"value":"Catalyzes the interconversion of L-alanine and D-alanine. Also weakly active on serine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanine = D-alanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20249"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57972"}],"ecNumber":"5.1.1.1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10079072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12203980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12741835"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10079072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11886871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12741835"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9063881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9671513"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10079072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12741835"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"}],"value":"Inhibited by acetate and propionate. Irreversibly inhibited by cycloserine"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10079072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9063881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9671513"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.10"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Belongs to the alanine racemase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Alanine racemase","featureId":"PRO_0000114499"},{"type":"Active site","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"Proton acceptor; specific for D-alanine","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10502689"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15807525"}]},{"type":"Active site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Proton acceptor; specific for L-alanine","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10502689"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"15807525"}]},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11886871"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11886871"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11886871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9063881"}]},{"type":"Modified residue","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10079072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11886871"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12741835"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.10"}]},{"type":"Mutagenesis","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10502689"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"6.5-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10502689"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"100-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10194319"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"1000-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10194319"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["E"]}},{"type":"Mutagenesis","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"4-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10194319"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["K"]}},{"type":"Mutagenesis","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"5000-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["F"]}},{"type":"Mutagenesis","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"2000-fold decrease in activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15807525"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["S"]}},{"type":"Mutagenesis","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"54-fold increase in serine racemase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12203980"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"81-fold increase in serine racemase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12203980"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["N"]}},{"type":"Mutagenesis","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"51-fold increase in serine racemase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12203980"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["Q"]}},{"type":"Sequence conflict","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"in Ref. 3; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"VV","alternativeSequences":["PP"]}},{"type":"Sequence conflict","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"in Ref. 1; AAA22220","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"AGASRL","alternativeSequences":["RGPPP"]}},{"type":"Sequence conflict","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"in Ref. 1; AAA22220","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"WL","alternativeSequences":["V"]}},{"type":"Beta strand","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1XQK"}]},{"type":"Helix","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1SFT"}]},{"type":"Beta strand","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1XQL"}]},{"type":"Beta strand","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1L6F"}]},{"type":"Beta strand","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Helix","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]},{"type":"Beta strand","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1BD0"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"}],"references":[{"referenceNumber":1,"citation":{"id":"2835089","citationType":"journal article","authors":["Tanizawa K.","Ohshima A.","Scheidegger A.","Inagaki K.","Tanaka H.","Soda K."],"citationCrossReferences":[{"database":"PubMed","id":"2835089"},{"database":"DOI","id":"10.1021/bi00404a033"}],"title":"Thermostable alanine racemase from Bacillus stearothermophilus: DNA and protein sequence determination and secondary structure prediction.","publicationDate":"1988","journal":"Biochemistry","firstPage":"1311","lastPage":"1316","volume":"27"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"2496744","citationType":"journal article","authors":["Faraci W.S.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"2496744"},{"database":"DOI","id":"10.1021/bi00428a004"}],"title":"Mechanism of inactivation of alanine racemase by beta, beta, beta-trifluoroalanine.","publicationDate":"1989","journal":"Biochemistry","firstPage":"431","lastPage":"437","volume":"28"},"referencePositions":["PROTEIN SEQUENCE OF 31-43"]},{"referenceNumber":3,"citation":{"id":"3730360","citationType":"journal article","authors":["Badet B.","Inagaki K.","Soda K.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"3730360"},{"database":"DOI","id":"10.1021/bi00359a029"}],"title":"Time-dependent inhibition of Bacillus stearothermophilus alanine racemase by (1-aminoethyl)phosphonate isomers by isomerization to noncovalent slowly dissociating enzyme-(1-aminoethyl)phosphonate complexes.","publicationDate":"1986","journal":"Biochemistry","firstPage":"3275","lastPage":"3282","volume":"25"},"referencePositions":["PROTEIN SEQUENCE OF 36-43"]},{"referenceNumber":4,"citation":{"id":"10194319","citationType":"journal article","authors":["Sun S.","Toney M.D."],"citationCrossReferences":[{"database":"PubMed","id":"10194319"},{"database":"DOI","id":"10.1021/bi982924t"}],"title":"Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase.","publicationDate":"1999","journal":"Biochemistry","firstPage":"4058","lastPage":"4065","volume":"38"},"referencePositions":["MUTAGENESIS OF ARG-219"]},{"referenceNumber":5,"citation":{"id":"10502689","citationType":"journal article","authors":["Watanabe A.","Yoshimura T.","Mikami B.","Esaki N."],"citationCrossReferences":[{"database":"PubMed","id":"10502689"},{"database":"DOI","id":"10.1093/oxfordjournals.jbchem.a022517"}],"title":"Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine.","publicationDate":"1999","journal":"J. Biochem.","firstPage":"781","lastPage":"786","volume":"126"},"referencePositions":["FUNCTION","ACTIVE SITES","MUTAGENESIS"]},{"referenceNumber":6,"citation":{"id":"12203980","citationType":"journal article","authors":["Patrick W.M.","Weisner J.","Blackburn J.M."],"citationCrossReferences":[{"database":"PubMed","id":"12203980"},{"database":"DOI","id":"10.1002/1439-7633(20020802)3:8<789::aid-cbic789>3.0.co;2-d"}],"title":"Site-directed mutagenesis of Tyr354 in Geobacillus stearothermophilus alanine racemase identifies a role in controlling substrate specificity and a possible role in the evolution of antibiotic resistance.","publicationDate":"2002","journal":"ChemBioChem","firstPage":"789","lastPage":"792","volume":"3"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF TYR-354"]},{"referenceNumber":7,"citation":{"id":"9063881","citationType":"journal article","authors":["Shaw J.P.","Petsko G.A.","Ringe D."],"citationCrossReferences":[{"database":"PubMed","id":"9063881"},{"database":"DOI","id":"10.1021/bi961856c"}],"title":"Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution.","publicationDate":"1997","journal":"Biochemistry","firstPage":"1329","lastPage":"1342","volume":"36"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE","COFACTOR","SUBUNIT","PYRIDOXAL PHOSPHATE AT LYS-39","SEQUENCE REVISION"]},{"referenceNumber":8,"citation":{"id":"9671513","citationType":"journal article","authors":["Stamper C.G.","Morollo A.A.","Ringe D."],"citationCrossReferences":[{"database":"PubMed","id":"9671513"},{"database":"DOI","id":"10.1021/bi980692s"}],"title":"Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine.","publicationDate":"1998","journal":"Biochemistry","firstPage":"10438","lastPage":"10445","volume":"37"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND L-ALA PHOSPHONATE","COFACTOR","ACTIVE SITE"]},{"referenceNumber":9,"citation":{"id":"10079072","citationType":"journal article","authors":["Morollo A.A.","Petsko G.A.","Ringe D."],"citationCrossReferences":[{"database":"PubMed","id":"10079072"},{"database":"DOI","id":"10.1021/bi9822729"}],"title":"Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase.","publicationDate":"1999","journal":"Biochemistry","firstPage":"3293","lastPage":"3301","volume":"38"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND PROPIONATE","CATALYTIC ACTIVITY","SUBUNIT","COFACTOR","PYRIDOXAL PHOSPHATE AT LYS-39","ACTIVITY REGULATION","CARBOXYLATION AT LYS-129"],"referenceComments":[{"value":"ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923 / NCTC 10339 / R-35646 / VKM B-510","type":"STRAIN"}]},{"referenceNumber":10,"citation":{"id":"CI-79D9TFLQQQSDM","citationType":"submission","authors":["Stamper G.F.","Ringe D."],"title":"Crystal structure of alanine racemase in complex with D-alanine phosphonate.","publicationDate":"SEP-2000","submissionDatabase":"PDB data bank"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH D-ALANINE PHOSPHONATE","CARBOXYLATION AT LYS-129"]},{"referenceNumber":11,"citation":{"id":"11886871","citationType":"journal article","authors":["Watanabe A.","Yoshimura T.","Mikami B.","Hayashi H.","Kagamiyama H.","Esaki N."],"citationCrossReferences":[{"database":"PubMed","id":"11886871"},{"database":"DOI","id":"10.1074/jbc.m201615200"}],"title":"Reaction mechanism of alanine racemase from Bacillus stearothermophilus: x-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine.","publicationDate":"2002","journal":"J. Biol. Chem.","firstPage":"19166","lastPage":"19172","volume":"277"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH N-(5'-PHOSPHOPYRIDOXYL)-D-ALANINE AND N-(5'-PHOSPHOPYRIDOXYL)-L-ALANINE","COFACTOR","ACTIVE SITE","PYRIDOXAL PHOSPHATE AT LYS-39","CARBOXYLATION AT LYS-129"]},{"referenceNumber":12,"citation":{"id":"12741835","citationType":"journal article","authors":["Fenn T.D.","Stamper G.F.","Morollo A.A.","Ringe D."],"citationCrossReferences":[{"database":"PubMed","id":"12741835"},{"database":"DOI","id":"10.1021/bi027022d"}],"title":"A side reaction of alanine racemase: transamination of cycloserine.","publicationDate":"2003","journal":"Biochemistry","firstPage":"5775","lastPage":"5783","volume":"42"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND CYCLOSERINE","CATALYTIC ACTIVITY","ACTIVITY REGULATION","COFACTOR","ACTIVE SITE","CARBOXYLATION AT LYS-129"]},{"referenceNumber":13,"citation":{"id":"15807525","citationType":"journal article","authors":["Fenn T.D.","Holyoak T.","Stamper G.F.","Ringe D."],"citationCrossReferences":[{"database":"PubMed","id":"15807525"},{"database":"DOI","id":"10.1021/bi047842l"}],"title":"Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase.","publicationDate":"2005","journal":"Biochemistry","firstPage":"5317","lastPage":"5327","volume":"44"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH CYCLOSERINE AND PYRIDOXAL PHOSPHATE","COFACTOR","SUBUNIT","PYRIDOXAL PHOSPHATE AT LYS-39","MUTAGENESIS OF TYR-265","ACTIVITY REGULATION","ACTIVE SITE","CARBOXYLATION AT LYS-129"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M19142","properties":[{"key":"ProteinId","value":"AAA22220.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A29984","properties":[{"key":"EntryName","value":"A29984"}]},{"database":"PDB","id":"1BD0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"1EPV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B=2-388"}]},{"database":"PDB","id":"1FTX","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B=2-388"}]},{"database":"PDB","id":"1L6F","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"1L6G","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"1NIU","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"1SFT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"1XQK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"1XQL","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"2SFP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A/B=1-388"}]},{"database":"PDB","id":"3UW6","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.30 A"},{"key":"Chains","value":"A/B/C=1-388"}]},{"database":"PDB","id":"4ILS","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A/B/C=1-388"}]},{"database":"PDBsum","id":"1BD0","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1EPV","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1FTX","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1L6F","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1L6G","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1NIU","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1SFT","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1XQK","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"1XQL","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"2SFP","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"3UW6","properties":[{"key":"Description","value":"-"}]},{"database":"PDBsum","id":"4ILS","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P10724","properties":[{"key":"Description","value":"-"}]},{"database":"MDRepo","id":"P10724","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P10724","properties":[{"key":"Description","value":"-"}]},{"database":"ChEMBL","id":"CHEMBL1075086","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB02038","properties":[{"key":"GenericName","value":"D-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-N,O-cycloserylamide"}]},{"database":"DrugBank","id":"DB03801","properties":[{"key":"GenericName","value":"Lysine Nz-Carboxylic Acid"}]},{"database":"DrugBank","id":"DB01993","properties":[{"key":"GenericName","value":"N-(5'-Phosphopyridoxyl)-D-Alanine"}]},{"database":"DrugBank","id":"DB04467","properties":[{"key":"GenericName","value":"N-(5'-phosphopyridoxyl)-L-alanine"}]},{"database":"DrugBank","id":"DB03097","properties":[{"key":"GenericName","value":"PMP-hydroxyisoxazole, pyridoxamine-5-phosphate-hydroxyisoxazole"}]},{"database":"DrugBank","id":"DB03766","properties":[{"key":"GenericName","value":"Propanoic acid"}]},{"database":"DrugBank","id":"DB02142","properties":[{"key":"GenericName","value":"Pyridoxamine-5'-Phosphate"}]},{"database":"DrugBank","id":"DB03327","properties":[{"key":"GenericName","value":"{1-[(3-Hydroxy-Methyl-5-Phosphonooxy-Methyl-Pyridin-4-Ylmethyl)-Amino]-Ethyl}-Phosphonic Acid"}]},{"database":"BRENDA","id":"5.1.1.1","properties":[{"key":"OrganismId","value":"623"}]},{"database":"SABIO-RK","id":"P10724","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00042","properties":[{"key":"RectionId","value":"UER00497"}]},{"database":"EvolutionaryTrace","id":"P10724","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008784","properties":[{"key":"GoTerm","value":"F:alanine racemase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10079072"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12203980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12741835"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030632","properties":[{"key":"GoTerm","value":"P:D-alanine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00430","properties":[{"key":"EntryName","value":"PLPDE_III_AR"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.37.10:FF:000006","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.10:FF:000002","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.10","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.37.10","properties":[{"key":"EntryName","value":"Lyase, Ornithine Decarboxylase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01201","properties":[{"key":"EntryName","value":"Ala_racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000821","properties":[{"key":"EntryName","value":"Ala_racemase"}]},{"database":"InterPro","id":"IPR009006","properties":[{"key":"EntryName","value":"Ala_racemase/Decarboxylase_C"}]},{"database":"InterPro","id":"IPR011079","properties":[{"key":"EntryName","value":"Ala_racemase_C"}]},{"database":"InterPro","id":"IPR001608","properties":[{"key":"EntryName","value":"Ala_racemase_N"}]},{"database":"InterPro","id":"IPR020622","properties":[{"key":"EntryName","value":"Ala_racemase_pyridoxalP-BS"}]},{"database":"InterPro","id":"IPR029066","properties":[{"key":"EntryName","value":"PLP-binding_barrel"}]},{"database":"NCBIfam","id":"TIGR00492","properties":[{"key":"EntryName","value":"alr"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30511","properties":[{"key":"EntryName","value":"ALANINE RACEMASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30511:SF0","properties":[{"key":"EntryName","value":"ALANINE RACEMASE, CATABOLIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00842","properties":[{"key":"EntryName","value":"Ala_racemase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01168","properties":[{"key":"EntryName","value":"Ala_racemase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00992","properties":[{"key":"EntryName","value":"ALARACEMASE"}]},{"database":"SMART","id":"SM01005","properties":[{"key":"EntryName","value":"Ala_racemase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50621","properties":[{"key":"EntryName","value":"Alanine racemase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51419","properties":[{"key":"EntryName","value":"PLP-binding barrel"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00395","properties":[{"key":"EntryName","value":"ALANINE_RACEMASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNDFHRDTWAEVDLDAIYDNVENLRRLLPDDTHIMAVVKANAYGHGDVQVARTALEAGASRLAVAFLDEALALREKGIEAPILVLGASRPADAALAAQQRIALTVFRSDWLEEASALYSGPFPIHFHLKMDTGMGRLGVKDEEETKRIVALIERHPHFVLEGLYTHFATADEVNTDYFSYQYTRFLHMLEWLPSRPPLVHCANSAASLRFPDRTFNMVRFGIAMYGLAPSPGIKPLLPYPLKEAFSLHSRLVHVKKLQPGEKVSYGATYTAQTEEWIGTIPIGYADGWLRRLQHFHVLVDGQKAPIVGRICMDQCMIRLPGPLPVGTKVTLIGRQGDEVISIDDVARHLETINYEVPCTISYRVPRIFFRHKRIMEVRNAIGRGESSA","length":388,"molWeight":43593,"crc64":"F54AA581F135EA7A","md5":"884CA0D21AEAD2503A1BBB7FEF560CAE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":2,"Modified residue":2,"Mutagenesis":11,"Sequence conflict":3,"Beta strand":24,"Helix":20},"uniParcId":"UPI00001258E5"}}