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Database: UniProt
Entry: Q1RFC0
LinkDB: Q1RFC0
Original site: Q1RFC0 
ID   DXS_ECOUT               Reviewed;         620 AA.
AC   Q1RFC0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   01-OCT-2014, entry version 59.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315};
GN   OrderedLocusNames=UTI89_C0443;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C
CC       atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield
CC       1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC       deoxy-D-xylulose 5-phosphate + CO(2). {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose
CC       5-phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
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DR   EMBL; CP000243; ABE05944.1; -; Genomic_DNA.
DR   RefSeq; YP_539475.1; NC_007946.1.
DR   ProteinModelPortal; Q1RFC0; -.
DR   SMR; Q1RFC0; 3-620.
DR   STRING; 364106.UTI89_C0443; -.
DR   EnsemblBacteria; ABE05944; ABE05944; UTI89_C0443.
DR   GeneID; 3993086; -.
DR   KEGG; eci:UTI89_C0443; -.
DR   PATRIC; 18450555; VBIEscCol42261_0549.
DR   eggNOG; COG1154; -.
DR   HOGENOM; HOG000012988; -.
DR   KO; K01662; -.
DR   OMA; MSTIRQK; -.
DR   OrthoDB; EOG6BKJ6P; -.
DR   BioCyc; ECOL364106:GHPQ-438-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 3.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR005476; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 3.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN         1    620       1-deoxy-D-xylulose-5-phosphate synthase.
FT                                /FTId=PRO_0000256416.
FT   REGION      121    123       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      153    154       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       152    152       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       181    181       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      80     80       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     181    181       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     288    288       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     370    370       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
SQ   SEQUENCE   620 AA;  67603 MW;  D9DCB77CA75EA7BA CRC64;
     MSFDIAKYPT LALVDSTQEL RLLPKESLPK LCDELRRYLL DSVSRSSGHF ASGLGTVELT
     VALHYVYNTP FDQLIWDVGH QAYPHKILTG RRDKIGTIRQ KGGLHPFPWR GESEYDVLSV
     GHSSTSISAG IGIAVAAEKE GKNRRTVCVI GDGAITAGMA FEAMNHAGDI RPDMLVVLND
     NEMSISENVG ALNNHLAQLL SGKLYSSLRE GGKKVFSGVP PIKELLKRTE EHIKGMVVPG
     TLFEELGFNY IGPVDGHDVL GLITTLKNMR DLKGPQFLHI MTKKGRGYEP AEKDPITFHA
     VPKFDPSSGC LPKSSGGLPS YSKIFGDWLC ETAAKDNKLM AITPAMREGS GMVEFSRKFP
     DRYFDVAIAE QHAVTFAAGL AIGGYKPIVA IYSTFLQRAY DQVLHDVAIQ KLPVLFAIDR
     AGIVGADGQT HQGAFDLSYL RCIPEMVIMT PSDENECRQM LYTGYHYNDG PSAVRYPRGN
     AVGVELTPLE KLPIGKGIVK RRGEKLAILN FGTLMPEAAK VAESLNATLV DMRFVKPLDE
     ALILEMAASH EALVTVEENA IMGGAGSGVN EVLMAHRKPV PVLNIGLPDF FIPQGTQEEM
     RAELGLDAAG MEAKIKAWLA
//
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