ID Q63GX0_BACCZ Unreviewed; 389 AA.
AC Q63GX0;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 75.
DE SubName: Full=Alanine racemase;
DE EC=5.1.1.1;
GN Name=alr; OrderedLocusNames=BCE33L0226;
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L;
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU20007.1; -; Genomic_DNA.
DR RefSeq; YP_081841.1; NC_006274.1.
DR ProteinModelPortal; Q63GX0; -.
DR SMR; Q63GX0; 4-389.
DR STRING; 288681.BCZK0226; -.
DR EnsemblBacteria; AAU20007; AAU20007; BCE33L0226.
DR GeneID; 3023521; -.
DR KEGG; bcz:BCZK0226; -.
DR PATRIC; 18883666; VBIBacCer95304_0246.
DR eggNOG; COG0787; -.
DR KO; K01775; -.
DR OMA; FIAANKF; -.
DR ProtClustDB; CLSK915752; -.
DR BioCyc; BCER288681:GHG7-750-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.
SQ SEQUENCE 389 AA; 43649 MW; 68CA362CA4ED85A9 CRC64;
MEEAPFYRDT WVEVDLDAIY NNVTHIKEFI PSDVEIFAVV KGNAYGHDYV PVAKTALEAG
ATRLAVAFLD EALVLRRAGI TAPILVLGPS PPRDINVAAE NDVALTVFQK EWVDEAIKLW
DGSSTMKYHI NFDSGMGRIG IRERKELKGF LKSLEGAPFL ELEGVYTHFA TADEVETSYF
DKQYNTFLEQ LSWLKEFGVN PKFVHTANSA ATLRFQGITF NAVRIGIAMY GLSPSVEIRP
FLPFKLEPAL SLHTKVAHIK QVIKGDGISY NVTYRTKTEE WIATVAIGYA DGWLRRLQGF
EVLVNGKRVP IVGRVTMDQF MIHLPCEVPL GTKVTLIGRQ GDEYISATEV AEYSGTINYE
IITTISFRVP RIFIRNGKVV EVINYLNDI
//
