GenomeNet

Database: UniProt
Entry: Q9FCV2
LinkDB: Q9FCV2
Original site: Q9FCV2 
ID   ALR_LACRE               Reviewed;         375 AA.
AC   Q9FCV2;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   05-DEC-2018, entry version 84.
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;
OS   Lactobacillus reuteri.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 53608 / 1063;
RX   PubMed=11910493; DOI=10.1007/s00284-001-0030-8;
RA   Thompson A., Griffin H., Gasson M.J.;
RT   "Characterization of an alanine racemase gene from Lactobacillus
RT   reuteri.";
RL   Curr. Microbiol. 44:246-250(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. {ECO:0000305|PubMed:11910493}.
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; AJ278312; CAC03497.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q9FCV2; -.
DR   SMR; Q9FCV2; -.
DR   PRIDE; Q9FCV2; -.
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_0000114529.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    265    265       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     137    137       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     312    312       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;  41248 MW;  2912040451188DEB CRC64;
     MVEGWHRASR LVVDAAAIRQ NVKKEIERLD PQSELFAVVK ANGYGHGLIP VARYTEQAGA
     TGFCVAILDE ALTLREAGFA EPILVLGITN VKWAALAAEK NVSLTVGDVE WLTKAAPQLT
     AEHPLKVHLA LDTGMGRIGF QESDGLNQAA ELLTNDPRFV FEGVFTHFAT ADEKDPTYFN
     LQVDRFHKLV DTLPEKPRYV HVSNTATSLW HAACNGNLIR FGVGIYGMNP SGTVLEPPYD
     LQPAMTLESQ LSFSKLLKKG RSVSYGATYT VEQDEWIGTV PIGYADGYPR CLQGFHVLVD
     GHFCEIVGRV CMDQLMIRLP HEYPAGTSVI LAGKSQGKSI SMTDIADYAG TINYEITCGF
     TERIPRVYKN NDIVK
//
DBGET integrated database retrieval system