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Database: UniProt/TrEMBL
Entry: D3HFR2_STRG3
LinkDB: D3HFR2_STRG3
Original site: D3HFR2_STRG3 
ID   D3HFR2_STRG3            Unreviewed;       368 AA.
AC   D3HFR2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   26-NOV-2014, entry version 39.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|RuleBase:RU004247};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|RuleBase:RU004247};
GN   Name=alr {ECO:0000313|EMBL:CBI14377.1};
GN   OrderedLocusNames=GALLO_1886 {ECO:0000313|EMBL:CBI14377.1};
OS   Streptococcus gallolyticus (strain UCN34).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=637909 {ECO:0000313|EMBL:CBI14377.1, ECO:0000313|Proteomes:UP000001517};
RN   [1] {ECO:0000313|EMBL:CBI14377.1, ECO:0000313|Proteomes:UP000001517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCN34 {ECO:0000313|EMBL:CBI14377.1,
RC   ECO:0000313|Proteomes:UP000001517};
RX   PubMed=20139183; DOI=10.1128/JB.01659-09;
RA   Rusniok C., Couve E., Da Cunha V., El Gana R., Zidane N., Bouchier C.,
RA   Poyart C., Leclercq R., Trieu-Cuot P., Glaser P.;
RT   "Genome sequence of Streptococcus gallolyticus: insights into its
RT   adaptation to the bovine rumen and its ability to cause
RT   endocarditis.";
RL   J. Bacteriol. 192:2266-2276(2010).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|RuleBase:RU004247,
CC       ECO:0000256|SAAS:SAAS00119529}.
CC   -!- COFACTOR:
CC       Note=Pyridoxal phosphate. {ECO:0000256|HAMAP-Rule:MF_01201,
CC       ECO:0000256|SAAS:SAAS00119531};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|RuleBase:RU004247}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|RuleBase:RU004188}.
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DR   EMBL; FN597254; CBI14377.1; -; Genomic_DNA.
DR   RefSeq; YP_003431297.1; NC_013798.1.
DR   ProteinModelPortal; D3HFR2; -.
DR   EnsemblBacteria; CBI14377; CBI14377; GALLO_1886.
DR   GeneID; 8777262; -.
DR   KEGG; sga:GALLO_1886; -.
DR   PATRIC; 35287205; VBIStrGal150982_1876.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; YGHGLER; -.
DR   UniPathway; UPA00042; UER00497.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
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 {ECO:0000313|Proteomes:UP000001517};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00119528};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00119523}.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   368 AA;  39738 MW;  7E64C1DC37D58373 CRC64;
     MISSLHRPTK AVIDLDAICQ NIDAVKANIP QDKKAFAVVK ANAYGHGATS VAQAIHHLVD
     GFCVSNIDEA LELREAGIEE TILILGVIMP DEVALARDYH VTLTVASQEW LDLANEQGIS
     LAGLDVHLKV DSGMGRIGVR SLDEAENVIA NLKKAGANVA GIFTHFATAD EADDTKFNEQ
     LEFFTNLVNN LSDKPAIVHA SNSATSIWHS ETIFNLVRLG IVMYGLNPSG TELDLPYPLK
     PALSLESSLV HVKTIPAGAT VGYGATYTAQ KEEYIATVPI GYADGWTRDL QGFSVLVNGE
     FCEIVGRVSM DQITIRLPEK LPIGTKVTLI GQEGSKVISA TDLAQKRGTI NYEVLCLLSD
     RIPRVYSK
//
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