GenomeNet

Database: UniProt
Entry: B9DVI3
LinkDB: B9DVI3
Original site: B9DVI3 
ID   ALR_STRU0               Reviewed;         368 AA.
AC   B9DVI3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 62.
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=SUB1535;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A.,
RA   Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A.,
RA   Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N.,
RA   Whatmore A.M., Bentley S.D., Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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; AM946015; CAR43287.1; -; Genomic_DNA.
DR   RefSeq; WP_015911843.1; NC_012004.1.
DR   ProteinModelPortal; B9DVI3; -.
DR   SMR; B9DVI3; -.
DR   STRING; 218495.SUB1535; -.
DR   PRIDE; B9DVI3; -.
DR   EnsemblBacteria; CAR43287; CAR43287; SUB1535.
DR   GeneID; 24163089; -.
DR   KEGG; sub:SUB1535; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; SUBE218495:G1G1Y-1553-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000449; 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    368       Alanine racemase.
FT                                /FTId=PRO_1000164630.
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   368 AA;  40084 MW;  B532D22C6BB1960B CRC64;
     MISSLHRPTV ATVDLQAIRD NIKAVQEHIS STTKTFAVVK ANAYGHGAIQ VAKAVDEEVD
     AFCVSNLDEA LELRQAGIEK DILILGVILA NEIPLAIEHS ITITVASNEW LESAKACQKD
     LAQLHVHVKV DSGMGRIGVR SLEEANQLIA GLTKSGAHVD GIFTHFATAD EENTDKFHQQ
     LAFFTDLVNA LAIKPELVHA SNSATSLWHS DTIFNAVRLG IVIYGLNPSG KTLNLPYPLK
     PALSLSSRLV HIKKIKAGNT VGYGATYTAK TEEYVGTLPI GYADGWTRDM QGYSVIIDGH
     LCEIIGRVSM DQLTVRLPKA FDIGQEVTLI GQEGHQMISA TDIAEKRGTI NYEVLCLLSD
     RIPRHYIN
//
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