GenomeNet

Database: UniProt
Entry: B2GA65
LinkDB: B2GA65
Original site: B2GA65 
ID   ALR_LACF3               Reviewed;         373 AA.
AC   B2GA65;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   16-JAN-2019, entry version 65.
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=LAF_0211;
OS   Lactobacillus fermentum (strain NBRC 3956 / LMG 18251).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=334390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3956 / LMG 18251;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H.,
RA   Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H.,
RA   Kikuchi J., Masaoka T., Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and
RT   Lactobacillus fermentum reveal a genomic island for reuterin and
RT   cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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; AP008937; BAG26547.1; -; Genomic_DNA.
DR   RefSeq; WP_003684030.1; NC_010610.1.
DR   ProteinModelPortal; B2GA65; -.
DR   SMR; B2GA65; -.
DR   EnsemblBacteria; BAG26547; BAG26547; LAF_0211.
DR   GeneID; 6233484; -.
DR   KEGG; lfe:LAF_0211; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; LFER334390:G1G2I-243-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001697; 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.
FT   CHAIN         1    373       Alanine racemase.
FT                                /FTId=PRO_1000138606.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     140    140       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     315    315       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   373 AA;  40926 MW;  50D15A4F5382EBCA CRC64;
     MVSARLRKTD LVVDLKALGA NVQRQREQLA PGSRILAVVK ANAYGNGMVP VASALARAGV
     EGFCVALLDE AIELRDSGIQ ELVLVLGITP VEYAPLAAAQ GISLTVGSLE WLKNYQRLAK
     EEGIKQPLKV HLALDTGMGR IGFTTPEDFK EALQLVAAPC FEFEGIFTHF ATADEEDATY
     FERQRARFDD FMAVVTKRPP FVHVANSATG LWHQKSIVAN TIRMGISMYG ANPSGVGIKE
     SFPLEPVTSL VTHATYVKQL KAGESVSYGA TYTAKEDEWV ATLPVGYADG YPRRMQGFYV
     LVDGQRCEVL GRVCMDQMMV RLPKEYPVGT EAVLMGRSLD QEITVTDVAE YAHTINYEIL
     TGMGARLHRR YLG
//
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