AC MF_00315; DC Protein; auto TR HAMAP; MF_00315; -; 1; level=0 XX Names: DXP_synth XX ID DXS 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; XX 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). 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Note=Binds 1 thiamine pyrophosphate per subunit.; 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. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily. XX DR NCBIfam; TIGR00204; Dxs; 1; trigger=no DR PROSITE; PS00801; TRANSKETOLASE_1; 1; trigger=no DR PROSITE; PS00802; TRANSKETOLASE_2; 1; trigger=no XX KW Magnesium KW Metal-binding KW Transferase KW Thiamine pyrophosphate KW Isoprene biosynthesis KW Thiamine biosynthesis XX GO GO:0000287; F:magnesium ion binding GO GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity GO GO:0030976; F:thiamine pyrophosphate binding GO GO:0016114; P:terpenoid biosynthetic process GO GO:0009228; P:thiamine biosynthetic process XX FT From: DXS_ECOLI (P77488) FT BINDING 121..123 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: [GAS]-x-[SAT] FT BINDING 153..154 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: [GA]-[ASTG] FT BINDING 152 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: N FT BINDING 80 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: H FT BINDING 181 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: N FT BINDING 288 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Optional; Condition: [YFH] FT BINDING 370 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT Condition: E XX Size: 583-680; Related: None; Template: P77488; Q9RUB5; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in KITGR, STRAW, STRCO Plasmid: None Comments: Atypical sequences in BUCAP and LISMO with internal deletions not taken into account in size range and alignment XX # Revision 1.36 2023/06/01 //