AC MF_00183; DC Protein; auto TR HAMAP; MF_00183; -; 1; level=0 XX Names: DXP_reductoisom XX ID DXR DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase; DE Short=DXP reductoisomerase; DE EC=1.1.1.267; DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase; DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase; GN Name=dxr; XX CC -!- FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of CC 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- CC phosphate (MEP). CC -!- CATALYTIC ACTIVITY: CC Reaction=2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D- CC xylulose 5-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:13717, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57792, CC ChEBI:CHEBI:58262, ChEBI:CHEBI:58349; EC=1.1.1.267; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5- CC phosphate: step 1/6. case CC -!- SUBUNIT: Homodimer. end case CC -!- SIMILARITY: Belongs to the DXR family. XX DR Pfam; PF02670; DXP_reductoisom; 1; trigger=no DR NCBIfam; TIGR00243; Dxr; 1; trigger=no XX KW Isoprene biosynthesis KW Metal-binding KW Manganese KW Magnesium KW NADP KW Oxidoreductase XX GO GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity GO GO:0016114; P:terpenoid biosynthetic process XX FT From: DXR_ECOLI (P45568) FT BINDING 10 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: T FT BINDING 11 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: G FT BINDING 12 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: S FT BINDING 13 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: [IV] FT BINDING 36 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Optional; Condition: [GA] FT BINDING 37 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Optional; Condition: [KR] FT BINDING 38 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: N FT BINDING 124 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: [NQ] FT BINDING 125 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: K FT BINDING 126 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: E FT BINDING 150 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: D FT BINDING 151 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: S FT BINDING 152 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: E FT BINDING 152 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: E FT BINDING 186 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: S FT BINDING 209 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: H FT BINDING 215 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT Condition: G FT BINDING 222 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: S FT BINDING 227 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: N FT BINDING 228 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: [KR] FT BINDING 231 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT Condition: E FT BINDING 231 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT Group: 1; Condition: E XX Size: 356-455; Related: None; Template: P45568; Q9KGU6; Q9RCT1; Q9X5F2; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: in BACAN, BACCR, BACCZ, BACHK Plasmid: None Comments: Possible wrong start in MANSM, PASMU and STRCO XX # Revision 1.33 2023/06/01 //