ID ALR_STRA3 Reviewed; 366 AA.
AC Q8E3M9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 69.
DE RecName: Full=Alanine racemase;
DE EC=5.1.1.1;
GN Name=alr; OrderedLocusNames=gbs1728;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L.,
RA Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P.,
RA Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing
RT invasive neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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; AL766852; CAD47387.1; -; Genomic_DNA.
DR RefSeq; NP_736163.1; NC_004368.1.
DR HSSP; P10724; 1NIU.
DR ProteinModelPortal; Q8E3M9; -.
DR STRING; 211110.gbs1728; -.
DR EnsemblBacteria; CAD47387; CAD47387; CAD47387.
DR GeneID; 1029940; -.
DR KEGG; san:gbs1728; -.
DR PATRIC; 19639365; VBIStrAga3577_1769.
DR GenoList; gbs1728; -.
DR eggNOG; COG0787; -.
DR HOGENOM; HOG000031444; -.
DR KO; K01775; -.
DR OMA; IRLPKAY; -.
DR ProtClustDB; PRK00053; -.
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 1 366 Alanine racemase.
FT /FTId=PRO_1000066042.
FT ACT_SITE 40 40 Proton acceptor; specific for D-alanine
FT (By similarity).
FT ACT_SITE 263 263 Proton acceptor; specific for L-alanine
FT (By similarity).
FT BINDING 136 136 Substrate (By similarity).
FT BINDING 310 310 Substrate; via amide nitrogen (By
FT similarity).
FT MOD_RES 40 40 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 366 AA; 40064 MW; A2CDC66976DDA133 CRC64;
MISSYHRPTR ALIDLEAIAN NVKSVQEHIP SDKKTFAVVK ANAYGHGAVE VSKYIESIVD
GFCVSNLDEA IELRQAGIVK MILVLGVVMP EQVILAKNEN ITLTVASLEW LRLCQTSAVD
LSGLEVHIKV DSGMGRIGVR QLDEGNKLIS ELGESGASVK GIFTHFATAD EADNCKFNQQ
LTFFKDFISG LDNCPDLVHA SNSATSLWHS ETIFNAVRLG VVMYGLNPSG TDLDLPYPIN
PALSLESELV HVKQLHDGSQ VGYGATYQVT GDEFVGTVPI GYADGWTRDM QGFSVIVNGE
LCEIIGRVSM DQMTIRLPQK YTIGTKVTLI GQQGSCNITT TDVAQKRQTI NYEVLCLLSD
RIPRYY
//
