ID DXS_NOVAD Reviewed; 640 AA.
AC Q2GC13;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 01-MAY-2013, entry version 54.
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=Saro_0161;
OS Novosphingobium aromaticivorans (strain DSM 12444).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12444;
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., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000248; ABD24610.1; -; Genomic_DNA.
DR RefSeq; YP_495444.1; NC_007794.1.
DR ProteinModelPortal; Q2GC13; -.
DR STRING; 279238.Saro_0161; -.
DR EnsemblBacteria; ABD24610; ABD24610; Saro_0161.
DR GeneID; 3918296; -.
DR KEGG; nar:Saro_0161; -.
DR PATRIC; 22782900; VBINovAro50627_0167.
DR eggNOG; COG1154; -.
DR HOGENOM; HOG000012988; -.
DR KO; K01662; -.
DR OMA; GDIKPDM; -.
DR ProtClustDB; PRK05444; -.
DR BioCyc; NARO279238:GHBU-854-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 1 640 1-deoxy-D-xylulose-5-phosphate synthase.
FT /FTId=PRO_0000256448.
FT REGION 120 122 Thiamine pyrophosphate binding (By
FT similarity).
FT REGION 152 153 Thiamine pyrophosphate binding (By
FT similarity).
FT METAL 151 151 Magnesium (By similarity).
FT METAL 180 180 Magnesium (By similarity).
FT BINDING 79 79 Thiamine pyrophosphate (By similarity).
FT BINDING 180 180 Thiamine pyrophosphate (By similarity).
FT BINDING 289 289 Thiamine pyrophosphate (By similarity).
FT BINDING 371 371 Thiamine pyrophosphate (By similarity).
SQ SEQUENCE 640 AA; 68041 MW; 4D6FB8BB5C50A7CF CRC64;
MSQEPATPLL DTVKTPDDLR KLAPTQLRQL ADELRVEMIS AVGQTGGHLG SGLGVVELTV
AIHYVFNTPE DRLVWDVGHQ AYPHKILTGR RDRIRTLRQA GGLSGFTKRS ESEYDPFGTA
HSSTSISAAL GFAIANKLSG RLGKGIAVIG DGAMSAGMAY EAMNNAEAAG NRLIVILNDN
DMSIAPPVGG LSAYLARLVS SGPFLGLRDI ARRLSRKLPR PLHEAARKTD EFARGMAMGG
TLFEELGFYY VGPIDGHNID QLIPVLENVR DAAEGPCLIH VVTQKGKGYA PAEAAADKYH
GVQKFDVITG EQVKAKAAAP AYQNVFGETL AKLADADPTI CAITAAMPSG TGVDKFAKAH
PDRTFDVGIA EQHAVTFAAG LAAEGMRPFC AIYSTFLQRA FDQVVHDVAI QNLPVRFAID
RAGLVGADGA THAGSFDVTY LATLPNLVVM AAADEAELVH MTYTAALHDS GPIAFRYPRG
NGVGVPLPEV PERLEIGKGR IIRQGSKVAL LSLGTRLAEA LKAADQLDAR GLSTTVADLR
FAKPLDVALI RQLMTTHDVI VTVEEGSIGG LGAHVLTMAS DEGLVDGGLK IRTMRLPDLF
QDHDAPEKQY DEAGLNAPHI VDTVLKALRH NSAGVSEARA
//
