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DXS1_GEOSL
ID   DXS1_GEOSL              Reviewed;         637 AA.
AC   Q74FC3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase 1 {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXPS 1 {ECO:0000255|HAMAP-Rule:MF_00315};
GN   Name=dxs1 {ECO:0000255|HAMAP-Rule:MF_00315}; OrderedLocusNames=GSU0686;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(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}.
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DR   EMBL; AE017180; AAR34016.1; -; Genomic_DNA.
DR   RefSeq; NP_951743.1; NC_002939.5.
DR   RefSeq; WP_010941346.1; NC_002939.5.
DR   AlphaFoldDB; Q74FC3; -.
DR   SMR; Q74FC3; -.
DR   STRING; 243231.GSU0686; -.
DR   EnsemblBacteria; AAR34016; AAR34016; GSU0686.
DR   KEGG; gsu:GSU0686; -.
DR   PATRIC; fig|243231.5.peg.680; -.
DR   eggNOG; COG1154; Bacteria.
DR   HOGENOM; CLU_009227_1_4_7; -.
DR   InParanoid; Q74FC3; -.
DR   OMA; QVGYHAQ; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IBA:GO_Central.
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:0016744; F:transketolase or transaldolase activity; IBA:GO_Central.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central.
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;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..637
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase 1"
FT                   /id="PRO_0000256424"
FT   BINDING         74
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         115..117
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         147..148
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         175
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         286
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         368
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   637 AA;  68013 MW;  C43DB7CCDC3BD7C1 CRC64;
     MSTLLDTITC PADLKKIPRD QLPALAEEIR AFLLETVSRT GGHLASNLGV VELSIALHYC
     FDSPTDRFVW DVGHQAYTHK ILTGRRDRFH TQRQYGGISG FPKRSESSHD AFDTGHSSTS
     ISAGLGMAMA RELRGGSNKV VAVIGDGSMT GGIAFEALNQ AGHLKKNLIV VLNDNEMSIS
     PNVGAFSSFV SRKLTGSYFR ELKKEVQGLL QNIPAIGKDI LQFARRAENS LKGFLTPGML
     FEALGFDYIG PIQGHNLPQL LEVFENARGL DGPVVVHVMT TKGKGYVPAE TNPSAFHGVG
     PFDVATGKTT GSKPGAASYT GIFGDTLAQL ARENEKIVAI TAAMPDGTGL TGFAKEFPER
     FFDVGIAEQH AVTFAAGLAA EGFRPVTAIY STFLQRAYDQ VFHDVCLQNL PVVFALDRGG
     VVGDDGPTHH GVFDLSYLRH LPGMTLMAPK DENELRHMLK TAVSHDGPIA LRYPRGAGCG
     IPLDQELREI PIGTGEILAE GDDVAIIAIG ITVLPALEAA RTLAEKGIRA TVINARFVKP
     LDREMILQAA RRTGCIITAE ENALQGGFGS AVLELLADEG MTGVRVKRLG IPDRFVEQGP
     QPQLRADLGI DAAGIAAATE AFLAAKGAPA PALSMVK
 
 
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