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Database: UniProt
Entry: Q1QU82
LinkDB: Q1QU82
Original site: Q1QU82 
ID   ALR_CHRSD               Reviewed;         364 AA.
AC   Q1QU82;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   13-FEB-2019, entry version 87.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=Csal_2629;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W.,
RA   Detter J.C., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Vargas C., Nieto J.J.,
RA   Kyrpides N.C., Ivanova N., Goker M., Klenk H.P., Csonka L.N.,
RA   Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CP000285; ABE59976.1; -; Genomic_DNA.
DR   RefSeq; WP_011507922.1; NC_007963.1.
DR   ProteinModelPortal; Q1QU82; -.
DR   SMR; Q1QU82; -.
DR   STRING; 290398.Csal_2629; -.
DR   EnsemblBacteria; ABE59976; ABE59976; Csal_2629.
DR   KEGG; csa:Csal_2629; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; CSAL290398:G1GJB-2688-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000239; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    364       Alanine racemase.
FT                                /FTId=PRO_1000065978.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     131    131       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     304    304       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   364 AA;  39714 MW;  7B5D6BC750957BDD CRC64;
     MSRPLIADID LDALRRNYCL ARDQAPHSRA IAVVKADAYG HGAVACADAL RDLAPAFAVA
     CLEEALTLRE AGITQPIVLL EGFFDAAELS LIDAHRLWTA VHSDWQIDAL LAYRPRQPIP
     TWLKLDSGMH RLGFAPEAFE ARWQRLAAAT EHVTDLHLMT HFATADALDA AYFRRQMACI
     ASLRQRLEAP VCLANSPATL AWPEAHGDWN RPGVMLYGSD PLEGANDASR ALEPVMTLRS
     EIIAVRELAE GEAVGYGGRW RASRPSRIGV VAGGYGDGYD RHARDGTPVL VEGQRVPLAG
     KVSMDMLTVD LTELPEAGIG SPVVLWGEGL PIDEVARHCD TISYTLMTGV LPRVPRRYRN
     AETG
//
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