ID   ALR_BORA1               Reviewed;         374 AA.
AC   Q2KXU7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Alanine racemase;
DE            EC=5.1.1.1;
GN   Name=alr; OrderedLocusNames=BAV2416;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50026.1; -; Genomic_DNA.
DR   RefSeq; YP_786930.1; -.
DR   GeneID; 6265961; -.
DR   GenomeReviews; AM167904_GR; BAV2416.
DR   KEGG; bav:BAV2416; -.
DR   NMPDR; fig|521.1.peg.60; -.
DR   HOGENOM; Q2KXU7; -.
DR   OMA; Q2KXU7; TGLKPAM.
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    374       Alanine racemase.
FT                                /FTId=PRO_1000065971.
FT   ACT_SITE     44     44       Proton acceptor; specific for D-alanine
FT                                (By similarity).
FT   ACT_SITE    269    269       Proton acceptor; specific for L-alanine
FT                                (By similarity).
FT   MOD_RES      44     44       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   374 AA;  39188 MW;  94E4487AA5D789F2 CRC64;
     MPRPIFALIS PTALRHNLSV VRQHLNRAAV AAGGVPPSIW AVIKANAYGH GIERALRAFS
     EAQGLAMLDI EEAVRCREAG WAGPILLLEG FFTPQDIDLL DRYHISTAVH CQEQLDMLAR
     ARPSHRINAM VKLNSGMNRL GFSPQAYGAA FEAAQALMRD GVLGSVGKMT HFATADGPQG
     PQWQWEVFQA ATQGLPGPVS VCNSAATLRY PELAAGPGAT HWVRPGICLY GASPFSDTPA
     AAFGLRPAMT LRAEIIGVQQ VSPGQTVGYG ATFAASKAMR VGVVSCGYAD GYPRHCATGT
     PVTVNGVATR LLGRVSMDMM MVDLDPVPAA GVGAPVVLWG EGGPDVDAVA AAGGTIGYEL
     LTALAARVPV RDAS
//