ID DXR_OLEA2 Reviewed; 407 AA. AC Q313H2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE Short=DXP reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE EC=1.1.1.267 {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00183}; DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00183}; GN Name=dxr {ECO:0000255|HAMAP-Rule:MF_00183}; GN OrderedLocusNames=Dde_1123; OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) OS (Desulfovibrio alaskensis). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Oleidesulfovibrio. OX NCBI_TaxID=207559; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20; RX PubMed=21685289; DOI=10.1128/jb.05400-11; RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L., RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R., RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S., RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.; RT "Complete genome sequence and updated annotation of Desulfovibrio RT alaskensis G20."; RL J. Bacteriol. 193:4268-4269(2011). 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). {ECO:0000255|HAMAP-Rule:MF_00183}. 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00183}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00183}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00183}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00183}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5- CC phosphate: step 1/6. {ECO:0000255|HAMAP-Rule:MF_00183}. CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000255|HAMAP- CC Rule:MF_00183}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000112; ABB37924.1; -; Genomic_DNA. DR AlphaFoldDB; Q313H2; -. DR SMR; Q313H2; -. DR STRING; 207559.Dde_1123; -. DR KEGG; dde:Dde_1123; -. DR eggNOG; COG0743; Bacteria. DR HOGENOM; CLU_035714_4_0_7; -. DR UniPathway; UPA00056; UER00092. DR Proteomes; UP000002710; Chromosome. DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0070402; F:NADPH binding; IEA:InterPro. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1740.10; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00183; DXP_reductoisom; 1. DR InterPro; IPR003821; DXP_reductoisomerase. DR InterPro; IPR013644; DXP_reductoisomerase_C. DR InterPro; IPR013512; DXP_reductoisomerase_N. DR InterPro; IPR026877; DXPR_C. DR InterPro; IPR036169; DXPR_C_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR00243; Dxr; 1. DR PANTHER; PTHR30525; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE; 1. DR PANTHER; PTHR30525:SF0; 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, CHLOROPLASTIC; 1. DR Pfam; PF08436; DXP_redisom_C; 1. DR Pfam; PF02670; DXP_reductoisom; 1. DR Pfam; PF13288; DXPR_C; 1. DR PIRSF; PIRSF006205; Dxp_reductismrs; 1. DR SUPFAM; SSF69055; 1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 3: Inferred from homology; KW Isoprene biosynthesis; Manganese; Metal-binding; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..407 FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase" FT /id="PRO_1000020255" FT BINDING 27 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 28 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 29 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 30 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 53 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 54 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 55 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 140 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 141 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 142 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 166 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 167 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 168 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 168 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 192 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 215 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 221 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 228 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 233 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 234 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 237 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 237 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" SQ SEQUENCE 407 AA; 43573 MW; 7C196C23DA5135E3 CRC64; MNGYISPLPD AAWNSRFPRS LVLLGSTGSI GTSALRVVER QPELFRITAL AGARNVRLLA RQAAAYRPPH LAVINGNAAD ELASLLPAGY RPRIHTGQEG YEFLAALPEA DCVLSAQVGA AGLRATVAAA RAGKTIALAN KESLVLAGGL IRRLCHETGA SVLPVDSEHN AIFQALQGHD AAQMRRIILT ASGGPFRGRD RTFLQSVTRE QALNHPNWSM GAKISIDSAT LMNKGLEVIE ACHLYNAPLE KVEVVVHPQS IIHSLVEYND GSQIAHMGTP DMRIAIAYCL GWPRVMHTGV EPLDLLSVGS LTFESPDISL FPCLELARKA YAGGNGLPVV LNAANEVAVD LFLQGAIAFL DIPRLIEAAM QAHDAAPHQN MYDEVESILT LDKTTRRVTA DLAGARG //