ID E8VAB8_BACST Unreviewed; 389 AA.
AC E8VAB8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 01-MAY-2013, entry version 20.
DE SubName: Full=Alanine racemase;
GN OrderedLocusNames=BSn5_13950;
OS Bacillus subtilis (strain BSn5).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=936156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSn5;
RX PubMed=21317323; DOI=10.1128/JB.00129-11;
RA Deng Y., Zhu Y., Wang P., Zhu L., Zheng J., Li R., Ruan L., Peng D.,
RA Sun M.;
RT "Complete genome sequence of Bacillus subtilis BSn5, an endophytic
RT bacterium of Amorphophallus konjac with antimicrobial activity to
RT plant pathogen Erwinia carotovora subsp. carotovora.";
RL J. Bacteriol. 193:2070-2071(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BSn5;
RA Deng Y., Sun M.;
RT "Complete Genome Sequence of Bacillus Subtilis BSn5, a Strain of
RT Plant-associated Bacterium with Antimicrobial Activity to Soil-borne
RT Plant Pathogens.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002468; ADV95398.1; -; Genomic_DNA.
DR RefSeq; YP_004206425.1; NC_014976.1.
DR ProteinModelPortal; E8VAB8; -.
DR SMR; E8VAB8; 4-382.
DR EnsemblBacteria; ADV95398; ADV95398; BSn5_13950.
DR GeneID; 10183488; -.
DR KEGG; bsn:BSn5_13950; -.
DR PATRIC; 46872934; VBIBacSub180317_2847.
DR HOGENOM; HOG000031444; -.
DR KO; K01775; -.
DR BioCyc; BSUB936156:GHCY-2841-MONOMER; -.
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; 43265 MW; 4802B7C182ACCD58 CRC64;
MSTKPFYRDT WAEIDLSAIK ENVSNMKKHI GEHVHLMAVV KANAYGHGDA ETAKAALDAG
ASCLAVAILD EAISLRKKGL KAPILVLGAV PPEYVAIAAE YDVTLTGYSV EWLQEAARHT
KKGSLHFHLK VDTGMNRLGV KTEEEVQNVM AILDRNPRLK CKGVFTHFAT ADEKERGYFL
MQFERFKELI APLPLKNLMV HCANSAAGLR LKKGFFNAVR FGIGMYGLRP SADMSDEIPF
QLRPAFTLHS TLSHVKLIRK GESVSYGAEY TAEKDTWIGT VPVGYADGWL RKLKGTDILV
KGKRLKIAGR ICMDQFMVEL DQEYPPGTKV TLIGRQGDEY ISMDEIAGRL ETINYEVACT
ISSRVPRMFL ENGSIMEVRN PLLQVNISN
//
