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Database: UniProt
Entry: C0M6I5
LinkDB: C0M6I5
Original site: C0M6I5 
ID   ALR_STRE4               Reviewed;         366 AA.
AC   C0M6I5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   19-FEB-2014, entry version 41.
DE   RecName: Full=Alanine racemase;
DE            EC=5.1.1.1;
GN   Name=alr; OrderedLocusNames=SEQ_0437;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K.,
RA   Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K.,
RA   Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K.,
RA   Aanensen D.M., Spratt B.G., Jolley K.A., Maiden M.C.J., Kehoe M.,
RA   Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J.,
RA   Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids (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   -!- SIMILARITY: Belongs to the alanine racemase family.
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DR   EMBL; FM204883; CAW92611.1; -; Genomic_DNA.
DR   RefSeq; YP_002745820.1; NC_012471.1.
DR   ProteinModelPortal; C0M6I5; -.
DR   STRING; 553482.SEQ_0437; -.
DR   EnsemblBacteria; CAW92611; CAW92611; SEQ_0437.
DR   GeneID; 7696299; -.
DR   KEGG; seu:SEQ_0437; -.
DR   PATRIC; 19645626; VBIStrEqu13040_0438.
DR   eggNOG; COG0787; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; ITMDQLM; -.
DR   OrthoDB; EOG6PP9NJ; -.
DR   ProtClustDB; PRK00053; -.
DR   BioCyc; SEQU553482:GJOY-453-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 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   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   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    366       Alanine racemase.
FT                                /FTId=PRO_1000164627.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine
FT                                (By similarity).
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine
FT                                (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     310    310       Substrate; via amide nitrogen (By
FT                                similarity).
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   366 AA;  40169 MW;  93BF7447BF1BA825 CRC64;
     MISSLHRPTV ARVDLEAIRA NIDHIHQHIP KKVRTYAVVK ANAYGHGAVA VSKAVEDQVD
     GYCVSNLDEA LELRQAGIDK EILILGVILA SELQLAIKHQ LTITVASLEW LELAKKESVD
     FSQLHVHVKV DSGMGRIGVR SLAEANQLIS ILSDMGVQLD GIFTHFATAD DSDHAMFDKQ
     LTFFKQLVEQ LDKRPALVHA SNSATSLWHS ETIFNAIRLG IVIYGLNPSG NSLSLPCPLK
     EALSLESRLV HVKQIQAGDS VGYGASYVAA EPEYVGTLPI GYADGWTRNM QGFKVLVEGE
     FCDIIGRVSM DQLTIRLPKA YPIGTKVTLI GQQGKQVITA TDVADYRGTI NYEVLCLLSD
     RIPREY
//
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