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Database: UniProt
Entry: Q1GBP6
LinkDB: Q1GBP6
Original site: Q1GBP6 
ID   ALR_LACDA               Reviewed;         376 AA.
AC   Q1GBP6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   05-DEC-2018, entry version 83.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=Ldb0360;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM
OS   20081 / JCM 1002 / NBRC 13953 / NCIMB 11778).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / JCM 1002 / NBRC 13953 / NCIMB 11778;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K.,
RA   Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V.,
RA   Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T.,
RA   Gibrat J.-F., Bessieres P., Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals
RT   extensive and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CR954253; CAI97198.1; -; Genomic_DNA.
DR   RefSeq; WP_011543628.1; NZ_JQAV01000001.1.
DR   ProteinModelPortal; Q1GBP6; -.
DR   SMR; Q1GBP6; -.
DR   STRING; 390333.Ldb0360; -.
DR   EnsemblBacteria; CAI97198; CAI97198; Ldb0360.
DR   GeneID; 4083551; -.
DR   KEGG; ldb:Ldb0360; -.
DR   PATRIC; fig|390333.13.peg.428; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; LDEL390333:LDB_RS01515-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001259; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   InterPro; IPR029066; PLP-binding_barrel.
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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    376       Alanine racemase.
FT                                /FTId=PRO_1000065998.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    270    270       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     317    317       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   376 AA;  41333 MW;  7CC9E0683824AAA6 CRC64;
     MITAVNRPAA LHINLAAIKE NTRQAKAHLK PGQKLFCVVK ANAYGHGAAR LAPVMEEAGA
     DGFCVAMLDE GLELRRAQIV KPILVLGLQP AEEAALAAAN DISLPVSSLD WLKKAEKVLR
     KEGLQLKIHL AIDSGMGRIG FSEDEDFKAV NEYLQGNDAF FVEGMFTHFA SADSADASYF
     DYQVKRFKHM ESLLTVKPKW IHVDNTAAIL FDKDVASDIV RFGIGLYGLN PSSAPGSRDL
     EPAFALKPAM SFVSELTYVK QIHKGYGVGY GSTHIAEEDE WIGTVPVGYA DGWIRKFQGF
     KVKVGDTYCP IVGRVCMDQF MVLLPKEVPA GTPVELISAD PAAPNSLRRA ADWLDTIHYE
     VACQFNDRLD RIYDNE
//
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