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Database: UniProt
Entry: Q8DSF4
LinkDB: Q8DSF4
Original site: Q8DSF4 
ID   ALR_STRMU               Reviewed;         371 AA.
AC   Q8DSF4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-DEC-2018, entry version 99.
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=SMU_1834;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-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; AE014133; AAN59457.1; -; Genomic_DNA.
DR   RefSeq; NP_722151.1; NC_004350.2.
DR   RefSeq; WP_002263464.1; NC_004350.2.
DR   ProteinModelPortal; Q8DSF4; -.
DR   SMR; Q8DSF4; -.
DR   STRING; 210007.SMU_1834; -.
DR   EnsemblBacteria; AAN59457; AAN59457; SMU_1834.
DR   GeneID; 1029043; -.
DR   KEGG; smu:SMU_1834; -.
DR   PATRIC; fig|210007.7.peg.1637; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   PhylomeDB; Q8DSF4; -.
DR   BioCyc; SMUT210007:G1FZX-1735-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
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; Reference proteome.
FT   CHAIN         1    371       Alanine racemase.
FT                                /FTId=PRO_1000066044.
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   371 AA;  40420 MW;  7D070156A4383910 CRC64;
     MIASYHRPTT ALVHLDRIKF NIEQVQHHIP KSAKTFAVVK ANAYGHGAVQ VAQAIQKQVD
     GFCVSNLDEA LELRQAGLND FILILGVLLP EEVALAKKEN ITITVADLDW FDKVQTENID
     LAGLSVHVKV DSGMGRIGVR STAEANQLIA GLQKAGATVN GIFTHFATAD EASTVKFSQQ
     LEMFTTLISQ LDYKPQTVHA SNSATSIWHS DTVMNAVRLG IVMYGLNPSG NALELPYEVK
     PALELTSALV QVKEVQAGDT VGYGATYTAS QAEIIGTVPV GYADGWTRDL QGFHVLVNGH
     YCEIVGRVSM DQITIRLPKA YPLGTKVTLI GQDGHETISA TDVAEKRETI NYEVLCLISD
     RVPRKYDKKF S
//
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