GenomeNet

Database: UniProt
Entry: Q8DY10
LinkDB: Q8DY10
Original site: Q8DY10 
ID   ALR_STRA5               Reviewed;         366 AA.
AC   Q8DY10;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-DEC-2018, entry version 92.
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=SAG1684;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R.,
RA   Radune D., Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S.,
RA   Carty H.A., Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M.,
RA   Iacobini E.T., Brettoni C., Galli G., Mariani M., Vegni F., Maione D.,
RA   Rinaudo D., Rappuoli R., Telford J.L., Kasper D.L., Grandi G.,
RA   Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an
RT   emerging human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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; AE009948; AAN00548.1; -; Genomic_DNA.
DR   RefSeq; NP_688675.1; NC_004116.1.
DR   RefSeq; WP_000625941.1; NC_004116.1.
DR   ProteinModelPortal; Q8DY10; -.
DR   SMR; Q8DY10; -.
DR   EnsemblBacteria; AAN00548; AAN00548; SAG1684.
DR   GeneID; 1014493; -.
DR   KEGG; sag:SAG1684; -.
DR   PATRIC; fig|208435.3.peg.1693; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; SAGA208435:G1FZP-1782-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000821; 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    366       Alanine racemase.
FT                                /FTId=PRO_1000066043.
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;  40064 MW;  A2CDC66976DDA133 CRC64;
     MISSYHRPTR ALIDLEAIAN NVKSVQEHIP SDKKTFAVVK ANAYGHGAVE VSKYIESIVD
     GFCVSNLDEA IELRQAGIVK MILVLGVVMP EQVILAKNEN ITLTVASLEW LRLCQTSAVD
     LSGLEVHIKV DSGMGRIGVR QLDEGNKLIS ELGESGASVK GIFTHFATAD EADNCKFNQQ
     LTFFKDFISG LDNCPDLVHA SNSATSLWHS ETIFNAVRLG VVMYGLNPSG TDLDLPYPIN
     PALSLESELV HVKQLHDGSQ VGYGATYQVT GDEFVGTVPI GYADGWTRDM QGFSVIVNGE
     LCEIIGRVSM DQMTIRLPQK YTIGTKVTLI GQQGSCNITT TDVAQKRQTI NYEVLCLLSD
     RIPRYY
//
DBGET integrated database retrieval system