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Database: UniProt/TrEMBL
Entry: B7IU32_BACC2
LinkDB: B7IU32_BACC2
Original site: B7IU32_BACC2 
ID   B7IU32_BACC2            Unreviewed;       389 AA.
AC   B7IU32;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   29-MAY-2013, entry version 37.
DE   RecName: Full=Alanine racemase;
DE            EC=5.1.1.1;
GN   Name=dal1; OrderedLocusNames=BCG9842_B5058;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
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DR   EMBL; CP001186; ACK97842.1; -; Genomic_DNA.
DR   RefSeq; YP_002443775.1; NC_011772.1.
DR   ProteinModelPortal; B7IU32; -.
DR   STRING; 405531.BCG9842_B5058; -.
DR   EnsemblBacteria; ACK97842; ACK97842; BCG9842_B5058.
DR   GeneID; 7184325; -.
DR   KEGG; bcg:BCG9842_B5058; -.
DR   PATRIC; 18896004; VBIBacCer50903_0234.
DR   eggNOG; COG0787; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; DELGHHF; -.
DR   ProtClustDB; CLSK915752; -.
DR   BioCyc; BCER405531:GI5L-253-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:EC.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 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   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; Racem_decarbox_C; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   ACT_SITE     41     41       Proton acceptor; specific for D-alanine
FT                                (By similarity).
FT   ACT_SITE    270    270       Proton acceptor; specific for L-alanine
FT                                (By similarity).
FT   BINDING     138    138       Substrate (By similarity).
FT   BINDING     317    317       Substrate; via amide nitrogen (By
FT                                similarity).
FT   MOD_RES      41     41       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   389 AA;  43758 MW;  BFAC5A471BD48227 CRC64;
     MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSDVEIFAVV KANAYGHDYV PVAKTALEAG
     ATRLAVAFLD EALVLRRAGI TVPILVLGPS PPRDVNVAAE NDVALTVFQK EWVDEAIKLW
     DGSSVMKFHI NFDSGMGRIG IRERKELKEF LRSLEGAPFL ELEGVYTHFA TADEVETSYF
     DKQYNTFLEQ LSWLKEFGVD PKFVHTANSA ATLRFQGITF NAVRIGIAMY GLSPSVEIRP
     FLPFELEPAL SLHTKVAHIK QVIKGDGISY NVTYRTKTEE WIATVAIGYA DGWLRRLQGF
     EVLINGKRVP IVGRVTMDQF MIHLPCEVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE
     IIATISFRVP RIFIRNGKVV EIINYLNNI
//
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