ID ALR_SHEB8 Reviewed; 358 AA.
AC A6WJ85;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Alanine racemase;
DE EC=5.1.1.1;
GN Name=alr; OrderedLocusNames=Shew185_0717;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Brettar I., Rodrigues J.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-2007) 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; CP000753; ABS06874.1; -; Genomic_DNA.
DR RefSeq; YP_001364937.1; NC_009665.1.
DR ProteinModelPortal; A6WJ85; -.
DR STRING; 402882.Shew185_0717; -.
DR EnsemblBacteria; ABS06874; ABS06874; Shew185_0717.
DR GeneID; 5372164; -.
DR KEGG; sbm:Shew185_0717; -.
DR PATRIC; 23457990; VBISheBal127872_0837.
DR eggNOG; COG0787; -.
DR HOGENOM; HOG000031446; -.
DR KO; K01775; -.
DR OMA; CIDEALT; -.
DR ProtClustDB; PRK00053; -.
DR BioCyc; SBAL402882:GJ99-741-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 GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 CHAIN 1 358 Alanine racemase.
FT /FTId=PRO_1000164611.
FT ACT_SITE 35 35 Proton acceptor; specific for D-alanine
FT (By similarity).
FT ACT_SITE 255 255 Proton acceptor; specific for L-alanine
FT (By similarity).
FT BINDING 130 130 Substrate (By similarity).
FT BINDING 303 303 Substrate; via amide nitrogen (By
FT similarity).
FT MOD_RES 35 35 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 358 AA; 38352 MW; 57E55165FC8F5FFC CRC64;
MNPFPRAEIS SSALQTNLAA LRQQAPASRV MAVVKANGYG HGLLNVANCL VSADGFGLAR
LDEALELRAG GVTARLLLLE GFFRATDLPL LVGHDIDTVV HHSSQLEMLE QTVLSKPVTV
WLKVDSGMHR LGFTPEQFST VYARLMACPN VAKPIHLMTH FACADEPDNS YTSVQMAAFN
SLTAGLPGFR TLANSAGALY WPQSQGDWIR PGIALYGVSP VTGDCGANHG LVPAMELVSQ
LIAVRDHKAN QPVGYGCFWT AKQDTRLGVV AIGYGDGYPR NAPEGTPVWV NGRRVPIVGR
VSMDMLTVDL GQDAQDKVGD SALLWGKALP VEEVAEHIGT IAYELVTKLT PRVAVCLA
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