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Database: UniProt
Entry: Q8Z688
LinkDB: Q8Z688
Original site: Q8Z688 
ID   ALR2_SALTI              Reviewed;         356 AA.
AC   Q8Z688;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   13-FEB-2019, entry version 113.
DE   RecName: Full=Alanine racemase, catabolic;
DE            EC=5.1.1.1;
GN   Name=dadX; Synonyms=dadB; OrderedLocusNames=STY1930, t1075;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized
CC       to pyruvate by DadA. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
DR   EMBL; AL513382; CAD05485.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO68741.1; -; Genomic_DNA.
DR   RefSeq; NP_456309.1; NC_003198.1.
DR   RefSeq; WP_000197904.1; NZ_UFRG01000003.1.
DR   ProteinModelPortal; Q8Z688; -.
DR   SMR; Q8Z688; -.
DR   STRING; 220341.STY1930; -.
DR   EnsemblBacteria; AAO68741; AAO68741; t1075.
DR   EnsemblBacteria; CAD05485; CAD05485; CAD05485.
DR   GeneID; 1248285; -.
DR   KEGG; stt:t1075; -.
DR   KEGG; sty:STY1930; -.
DR   PATRIC; fig|220341.7.peg.1947; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   BioCyc; GCF_001048035:AC754_RS11475-MONOMER; -.
DR   BioCyc; GCF_001048375:AC768_RS14295-MONOMER; -.
DR   BioCyc; GCF_001079465:ADV44_RS09240-MONOMER; -.
DR   BioCyc; GCF_001088345:AEZ18_RS15705-MONOMER; -.
DR   BioCyc; GCF_001095585:AD238_RS14670-MONOMER; -.
DR   BioCyc; GCF_001104165:AE704_RS14295-MONOMER; -.
DR   BioCyc; GCF_001104885:AEZ38_RS15020-MONOMER; -.
DR   BioCyc; GCF_001106745:AE121_RS09255-MONOMER; -.
DR   BioCyc; GCF_001118185:AE086_RS10380-MONOMER; -.
DR   BioCyc; GCF_001119245:AE140_RS10310-MONOMER; -.
DR   BioCyc; GCF_001121865:AE338_RS15255-MONOMER; -.
DR   BioCyc; GCF_001127485:AE735_RS10305-MONOMER; -.
DR   BioCyc; GCF_001135805:AEG73_RS14515-MONOMER; -.
DR   BioCyc; GCF_001148125:AEN24_RS07520-MONOMER; -.
DR   BioCyc; GCF_001148305:AEN67_RS12070-MONOMER; -.
DR   BioCyc; GCF_001157245:AER93_RS14540-MONOMER; -.
DR   BioCyc; GCF_001163025:AFA50_RS14570-MONOMER; -.
DR   BioCyc; GCF_001165785:AFA97_RS10380-MONOMER; -.
DR   BioCyc; GCF_001240865:ALC23_RS15555-MONOMER; -.
DR   BioCyc; GCF_001356455:AQJ76_RS14295-MONOMER; -.
DR   BioCyc; GCF_001357935:AQL34_RS23615-MONOMER; -.
DR   BioCyc; GCF_001359015:AQL50_RS23425-MONOMER; -.
DR   BioCyc; GCF_001360555:AQK88_RS14295-MONOMER; -.
DR   BioCyc; GCF_001361075:AQM75_RS09985-MONOMER; -.
DR   BioCyc; GCF_001362095:AQO19_RS10740-MONOMER; -.
DR   BioCyc; GCF_001362135:AQN73_RS15645-MONOMER; -.
DR   BioCyc; GCF_001362175:AQN68_RS14295-MONOMER; -.
DR   BioCyc; GCF_001362195:AQN87_RS02295-MONOMER; -.
DR   BioCyc; GCF_001362335:AQN99_RS12055-MONOMER; -.
DR   BioCyc; GCF_001364695:AQQ97_RS24040-MONOMER; -.
DR   BioCyc; GCF_900185485:CDZ80_RS09635-MONOMER; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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:0006522; P:alanine metabolic process; IEA:UniProtKB-UniRule.
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    356       Alanine racemase, catabolic.
FT                                /FTId=PRO_0000114560.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     130    130       Substrate. {ECO:0000250}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   356 AA;  38732 MW;  43DF23205EF25EE3 CRC64;
     MTRPIQASLD LQVMKQNLAI VRRAAPEARV WSVVKANAYG HGIERVWSAL GATDGFAMLN
     LEEAITLRER GWKGPILMLE GFFHAQDLEA YDTYRLTTCI HSNWQLKALQ NARLNAPLDI
     YVKVNSGMNR LGFQPERAQT VWQQLRAMRN VGEMTLMSHF AQADHPEGIG EAMRRIALAT
     EGLQCAYSLS NSAATLWHPQ AHYDWVRPGI ILYGASPSGQ WRDIADTGLK PVMTLSSEII
     GVQTLSAGER VGYGGGYSVT QEQRIGIVAA GYADGYPRHA PTGTPVLVDG IRTRTVGTVS
     MDMLAVDLTP CPQAGIGTPV ELWGKEIKVD DVASAAGTLG YGLLCAVAPR VPFVTT
//
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