GenomeNet

Database: UniProt
Entry: Q1IYK9
LinkDB: Q1IYK9
Original site: Q1IYK9 
ID   ALR_DEIGD               Reviewed;         355 AA.
AC   Q1IYK9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   16-JAN-2019, 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=Dgeo_1380;
OS   Deinococcus geothermalis (strain DSM 11300).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Daly M.J., Fredrickson J.K., Makarova K.S., Gaidamakova E.K.,
RA   Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM
RT   11300.";
RL   Submitted (APR-2006) 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; CP000359; ABF45675.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q1IYK9; -.
DR   SMR; Q1IYK9; -.
DR   STRING; 319795.Dgeo_1380; -.
DR   EnsemblBacteria; ABF45675; ABF45675; Dgeo_1380.
DR   KEGG; dge:Dgeo_1380; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002431; 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    355       Alanine racemase.
FT                                /FTId=PRO_1000065986.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    251    251       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     299    299       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   355 AA;  37475 MW;  C5D67E1FA1372C70 CRC64;
     MQEMQARAQA LISESALRSN LTALARQAGT QLLLPVKADA YGHGMEIVAR LAARHPAVWG
     FAVAVPREAA TLAALGLGKP ILLLTPPTLE EMGPLADLGV RLPVASLAEA EALPAHARAH
     LKVDTGMNRL GARPEEAVRV GQRLAERGLL EGAYTHFATA DEPDLSFARQ QFARFQEVLA
     ALPPVLAHAA NGGGVLSFGP LPSLSLARPG LASYGFAPAH LRGVAPLTPV MTLQARVTHV
     HAVYPGESVS YGGLWRATRK TIVATVGIGY ADGYPRNATG KACVLVRGEC RPVLGRICMD
     QCMVDVTDLE VRVGDWVEVW GTDKITVTDV AAWGGTVEYE VLTGLGARVE RVAAG
//
DBGET integrated database retrieval system