(data stored in ACNUC30630 zone)

SWISSPROT: DXS_TROW8

ID   DXS_TROW8               Reviewed;         629 AA.
AC   Q83I20;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 99.
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}; OrderedLocusNames=TW280;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC       and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC       xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC         xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:59776; EC=2.2.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00315};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC       phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; BX251410; CAD66954.1; -; Genomic_DNA.
DR   RefSeq; WP_011096234.1; NC_004551.1.
DR   SMR; Q83I20; -.
DR   PRIDE; Q83I20; -.
DR   EnsemblBacteria; CAD66954; CAD66954; TW280.
DR   GeneID; 29577816; -.
DR   KEGG; tws:TW280; -.
DR   HOGENOM; HOG000012986; -.
DR   KO; K01662; -.
DR   OMA; QVGYHAQ; -.
DR   BioCyc; GCF_000196075:G1EE9-301-MONOMER; -.
DR   UniPathway; UPA00064; UER00091.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02007; TPP_DXS; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43322; PTHR43322; 1.
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; 2.
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;
DR   PRODOM; Q83I20.
DR   SWISS-2DPAGE; Q83I20.
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Thiamine biosynthesis;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..629
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT                   /id="PRO_0000189167"
FT   REGION          119..121
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   REGION          151..152
FT                   /note="Thiamine pyrophosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   METAL           150
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   METAL           180
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         79
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         180
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         292
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         377
FT                   /note="Thiamine pyrophosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   629 AA;  68649 MW;  26576761E1316F8F CRC64;
     MCTKRQYGLL ESIRSPRDLD SFTPHQLDEL ECQVRDFLIQ SVAKTGGHLG SNLGVVELSI
     ALHRSFRSPE DCIIFDVGHQ CYVHKLITGR HDFKALRCKN GLSGYPSRHE SNHDIVENSH
     ASAALSWADG VSRARTLLGN DNYVIAVVGD GSLTGGMCWE ALNNISDDNN RRLVIVVNDN
     GRSYARTIGG IARFLNAVRA SKSYLWLRES SEAVFSHMGS PGRRLYQGIR GAIHGFLSRF
     SSSNKLFSNL DIRYLGPING HNRKALEKAF KQAKQYARPI IVHVITEKGH GYPPALEDAL
     DCLHTVGVID PSTGKSASVQ GQVRQDTWTG VFGEELLRLA ESNTNIVAVT AAMLHPTGLS
     MFAEKFPHRV FDVGIAEQHA VASAAGLAYE GLHPVVAIYS TFMNRAFDQV MMDVALHGAP
     VTFVLDRAGI TGPDGASHHG IWDLSLLRIV PGIKLYAPRD ASTLRNTLAL VCSEDCPTAI
     RFPRGSVCDD LPALRSLDDG IDVLYGSCDR EDIVIVAIGV MAHACVRAAQ LLAESGIEST
     VINPVCFWPL HRQVLARVSK AKLVVLAEEG AKSPGLGDYI AGRRLLEFVI PGDFQPQGSR
     DELLDAIGLN GEHIARKIKA RFNQIINCV
//

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