GenomeNet

Database: UniProt
Entry: B2G5M9
LinkDB: B2G5M9
Original site: B2G5M9 
ID   ALR_LACRJ               Reviewed;         375 AA.
AC   B2G5M9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   05-DEC-2018, 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=LAR_0245;
OS   Lactobacillus reuteri (strain JCM 1112).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
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; AP007281; BAG24761.1; -; Genomic_DNA.
DR   RefSeq; WP_003667248.1; NC_010609.1.
DR   ProteinModelPortal; B2G5M9; -.
DR   SMR; B2G5M9; -.
DR   EnsemblBacteria; BAG24761; BAG24761; LAR_0245.
DR   GeneID; 5189698; -.
DR   KEGG; lrf:LAR_0245; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; LREU557433:G1G2C-265-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
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   Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    375       Alanine racemase.
FT                                /FTId=PRO_1000138607.
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   375 AA;  41162 MW;  C28A06353B077B21 CRC64;
     MVNGRLRDTS LIVDLDALRH NIQEQKKVLP ENSKILAVVK ANAYGNGLIP VAQTAMTSGA
     SGLCVAILDE ALELRDNGIE AMTLVLGITS VEDALIAAQA GVSLTVGSLD WLEQYHQLAQ
     VAKPKKPLKV HLGIDSGMGR IGFTEVAAFK QAVKLLDSPE FEFEGMFTHF ATADSPDENY
     FNQQVQRWHQ FVASLAELPP YVHMANSATG LWHRETITAN TIRMGISMYG QNPSGRDLKL
     TLDLQPVSSL VSSISFVKQL KAGRSVSYGA TYTAEQDEWL ATLPIGYADG YPRCMTGYKV
     LVDGQFCDIA GRVCMDQMMI RLPKYYPVGT PVVLMGKSGD QEITATDLAE RAGTINYEIL
     TNISNRVHRI YRQSK
//
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