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   16-JUN-2009, entry version 27.
DE   RecName: Full=Alanine racemase;
DE            EC=5.1.1.1;
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].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the D-alanine required for cell wall
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
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DR   EMBL; CP000285; ABE59976.1; -; Genomic_DNA.
DR   RefSeq; YP_574675.1; -.
DR   GeneID; 4028157; -.
DR   GenomeReviews; CP000285_GR; Csal_2629.
DR   KEGG; csa:Csal_2629; -.
DR   NMPDR; fig|290398.4.peg.2420; -.
DR   HOGENOM; Q1QU82; -.
DR   OMA; Q1QU82; TGLKPAM.
DR   BioCyc; CSAL290398:CSAL_2629-MON; -.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:HAMAP.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_01201; -; 1.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR000821; Ala_racemase_reg.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate.
FT   CHAIN         1    364       Alanine racemase.
FT                                /FTId=PRO_1000065978.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine
FT                                (By similarity).
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine
FT                                (By similarity).
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
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
//