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 01-MAY-2013, entry version 36.
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; IRLPKAY; -.
DR ProtClustDB; PRK00053; -.
DR BioCyc; SEQU553482:GJOY-453-MONOMER; -.
DR UniPathway; UPA00042; UER00497.
DR GO; GO:0008784; F:alanine racemase activity; IEA:EC.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; Racem_decarbox_C; 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
//
