GenomeNet

Database: UniProt/SWISS-PROT
Entry: ALR_STRP3
LinkDB: ALR_STRP3
Original site: ALR_STRP3 
ID   ALR_STRP3               Reviewed;         366 AA.
AC   P0CZ56; Q8K5Z8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   28-FEB-2018, entry version 37.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=SpyM3_1563;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S.,
RA   Mammarella N.D., Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D.,
RA   Campbell D.S., Smith T.M., McCormick J.K., Leung D.Y.M.,
RA   Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus:
RT   phage-encoded toxins, the high-virulence phenotype, and clone
RT   emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AE014074; AAM80170.1; -; Genomic_DNA.
DR   RefSeq; WP_002995397.1; NC_004070.1.
DR   ProteinModelPortal; P0CZ56; -.
DR   SMR; P0CZ56; -.
DR   PRIDE; P0CZ56; -.
DR   EnsemblBacteria; AAM80170; AAM80170; SpyM3_1563.
DR   KEGG; spg:SpyM3_1563; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000564; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 2.
DR   Gene3D; 3.20.20.10; -; 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   InterPro; IPR029066; PLP-binding_barrel.
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   SUPFAM; SSF51419; SSF51419; 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_0000114584.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   366 AA;  39891 MW;  A68E7AF7E0AF9B95 CRC64;
     MISSFHRPTV ARVNLQAIKE NVASVQKHIP LGVKTYAVVK ADAYGHGAVQ VSKALLPQVD
     GYCVSNLDEA LQLRQAGIDK EILILGVLLP NELELAVANA ITVTIASLDW IALARLEKKE
     CQGLKVHVKV DSGMGRIGLR SSKEVNLLID SLKELGADVE GIFTHFATAD EADDTKFNQQ
     LQFFKKLIAG LEDKPRLVHA SNSATSIWHS DTIFNAVRLG IVSYGLNPSG SDLSLPFPLQ
     EALSLESSLV HVKMISAGDT VGYGATYTAK KSEYVGTVPI GYADGWTRNM QGFSVLVDGQ
     FCEIIGRVSM DQLTIRLSKA YPLGTKVTLI GSNQQKNIST TDIANYRNTI NYEVLCLLSD
     RIPRIY
//
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