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-MAY-2013, entry version 52.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase;
DE EC=2.2.1.7;
DE AltName: Full=1-deoxyxylulose-5-phosphate synthase;
DE Short=DXP synthase;
DE Short=DXPS;
GN Name=dxs; 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) (By similarity).
CC -!- CATALYTIC ACTIVITY: Pyruvate + D-glyceraldehyde 3-phosphate = 1-
CC deoxy-D-xylulose 5-phosphate + CO(2).
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC similarity).
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 -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
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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; GDIKPDM; -.
DR ProtClustDB; PRK05444; -.
DR BioCyc; ECOL364106:GHPQ-539-MONOMER; -.
DR UniPathway; UPA00064; UER00091.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA: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:HAMAP.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.920; -; 1.
DR HAMAP; MF_00315; DXP_synth; 1; -.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR InterPro; IPR015941; Transketolase-like_C.
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; SSF52922; Transketo_C_like; 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 (By
FT similarity).
FT REGION 153 154 Thiamine pyrophosphate binding (By
FT similarity).
FT METAL 152 152 Magnesium (By similarity).
FT METAL 181 181 Magnesium (By similarity).
FT BINDING 80 80 Thiamine pyrophosphate (By similarity).
FT BINDING 181 181 Thiamine pyrophosphate (By similarity).
FT BINDING 288 288 Thiamine pyrophosphate (By similarity).
FT BINDING 370 370 Thiamine pyrophosphate (By similarity).
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
//
