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Database: UniProt
Entry: Q39RJ8
LinkDB: Q39RJ8
Original site: Q39RJ8 
ID   ALR_GEOMG               Reviewed;         379 AA.
AC   Q39RJ8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   16-JAN-2019, entry version 88.
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=Gmet_2908;
OS   Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS-15 / ATCC 53774 / DSM 7210;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000148; ABB33126.1; -; Genomic_DNA.
DR   RefSeq; WP_004512844.1; NC_007517.1.
DR   ProteinModelPortal; Q39RJ8; -.
DR   SMR; Q39RJ8; -.
DR   STRING; 269799.Gmet_2908; -.
DR   PRIDE; Q39RJ8; -.
DR   EnsemblBacteria; ABB33126; ABB33126; Gmet_2908.
DR   KEGG; gme:Gmet_2908; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007073; 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    379       Alanine racemase.
FT                                /FTId=PRO_1000164597.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       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      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   379 AA;  41179 MW;  01C43A0EEAC66C70 CRC64;
     MDSRPTIAEI DLAALRHNFE QVQRAVPAGC GILAIVKADA YGHGFMDISR ELESLGVTAF
     GVAFLAEGIQ LRKSGIDRPV LILGGVYPGQ ERKCVGFNLS TAVFSLEQAR VLNDTAARLY
     RKAKIHVKID TGMGRLGVAA AEAPAFFREL REMKSLELEG IISHFASADE LDDDGRRFSD
     RQAAVFAQSV AEARSLGLDP RYVHIANSAA AFGMDLPFCN LVRPGIVLYG ALPSGDFEGK
     MALRPIMRLQ STVAMLKWVE PGTSISYARR YTAPDRRLIA SVPVGYADGY SRALTNRGEV
     LIRGTRAPVV GTVCMDWIMI DVTSVPGVAV GDEVTLLGCD RQGHCVRAEE LASWAGTIPY
     EIFCGISKRV PRVYLNATR
//
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