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Database: UniProt
Entry: Q2GC13
LinkDB: Q2GC13
Original site: Q2GC13 
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-OCT-2014, entry version 60.
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=Saro_0161;
OS   Novosphingobium aromaticivorans (strain DSM 12444 / F199).
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 / F199;
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). {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; 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; MSTIRQK; -.
DR   BioCyc; NARO279238:GHBU-161-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   Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN         1    640       1-deoxy-D-xylulose-5-phosphate synthase.
FT                                /FTId=PRO_0000256448.
FT   REGION      120    122       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   REGION      152    153       Thiamine pyrophosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   METAL       151    151       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   METAL       180    180       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00315}.
FT   BINDING      79     79       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     180    180       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     289    289       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
FT   BINDING     371    371       Thiamine pyrophosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00315}.
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
//
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