GenomeNet

Database: UniProt/TrEMBL
Entry: F0PTA9_BACT0
LinkDB: F0PTA9_BACT0
Original site: F0PTA9_BACT0 
ID   F0PTA9_BACT0            Unreviewed;       389 AA.
AC   F0PTA9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   03-APR-2013, entry version 16.
DE   SubName: Full=Alanine racemase;
GN   OrderedLocusNames=YBT020_01295;
OS   Bacillus thuringiensis subsp. finitimus (strain YBT-020).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=930170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBT-020;
RX   PubMed=21398543; DOI=10.1128/JB.00267-11;
RA   Zhu Y., Shang H., Zhu Q., Ji F., Wang P., Fu J., Deng Y., Xu C.,
RA   Ye W., Zheng J., Zhu L., Ruan L., Peng D., Sun M.;
RT   "Complete genome sequence of Bacillus thuringiensis serovar finitimus
RT   strain YBT-020.";
RL   J. Bacteriol. 193:2379-2380(2011).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002508; ADY19511.1; -; Genomic_DNA.
DR   RefSeq; YP_005563929.1; NC_017200.1.
DR   EnsemblBacteria; ADY19511; ADY19511; YBT020_01295.
DR   GeneID; 12187925; -.
DR   KEGG; btf:YBT020_01295; -.
DR   PATRIC; 47086044; VBIBacThu177620_0249.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
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.
SQ   SEQUENCE   389 AA;  43556 MW;  95EA3ADC68B15697 CRC64;
     MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSGVEIFAVV KGNAYGHDYV PVAKTALEAG
     ATRLAVAFLD EALVLRRAGI TAPILVLGPS PPRDINVAAE NDVALTVFQK EWVDEAIKLW
     DGSSTMKYHI NFDSGMGRIG IRERKELKGF LKSLEGAPFL ELEGVYTHFA TADEVETSYF
     DKQYNTFLEQ LSWLKEFGVN PKFVHTANSA ATLRFQGITF NAVRIGIAMY GLSPSVEIRP
     FLPLKLEPAL SLHTKVAHIK QVIKGDGISY NVTYRTKTEE WIATVAIGYA DGWLRRLQGF
     EVLVNGKRVP IVGRVTMDQF MIHLPCKVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE
     IITTISFRVP RIFIRNGKVV EVINYLNDI
//
DBGET integrated database retrieval system