ID   ALR_CLOPS               Reviewed;         386 AA.
AC   Q0SUN0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Alanine racemase;
DE            EC=5.1.1.1;
GN   Name=alr; OrderedLocusNames=CPR_0852;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
RA   DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
RA   Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
RA   Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
RA   Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
RA   Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
RA   Melville S.B., Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial
RT   pathogen, Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(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; CP000312; ABG85889.1; -; Genomic_DNA.
DR   RefSeq; YP_698177.1; -.
DR   GeneID; 4205106; -.
DR   GenomeReviews; CP000312_GR; CPR_0852.
DR   KEGG; cpr:CPR_0852; -.
DR   TIGR; CPR_0852; -.
DR   HOGENOM; Q0SUN0; -.
DR   OMA; Q0SUN0; NTVGYDR.
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    386       Alanine racemase.
FT                                /FTId=PRO_1000065981.
FT   ACT_SITE     38     38       Proton acceptor; specific for D-alanine
FT                                (By similarity).
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine
FT                                (By similarity).
FT   MOD_RES      38     38       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   386 AA;  42975 MW;  DDA02B0288CC844E CRC64;
     MDICVRPVWA EIDLDIIANN MKEIRNLVGE KEIIAVVKAN AYGHGALDIA STLLENGASR
     LAVAIITEAD ELRDAGITAP IMILGYTPIN FAENLINNEI EQTVYDVEYA KELSDFALKL
     GKKAKIHIAI DTGMGRIGFL PNEEGLNKVL EICSLPGVEV VGLFTHFSTS DEKDKTYTYE
     QFSKLTNFNK ALEDNGIHIP LKHASNSGAI MDLPETYLDG VRCGIISYGY YPSEEVKKEN
     LKLKPALTLK TNVAFVKELD EDMYVSYGRT YKTEKKSKIA TLPIGYADGY SRLLSGKAKV
     IIKGQFANVI GRVCMDQCMV DVTHIEDVKI GDEVILLGEE NGLKFDANDM AEIMGTINYE
     ILCMISHRVP RIYKKNNEIV KVRNYI
//