ID DXR_BURCJ Reviewed; 398 AA. AC B4ECM5; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 02-SEP-2026, entry version 94. 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=BceJ2315_20470; ORFNames=BCAL2085; OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; OC Burkholderia cepacia complex. OX NCBI_TaxID=216591; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / RC CF5610; RX PubMed=18931103; DOI=10.1128/jb.01230-08; RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D., RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S., RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K., RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D., RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R., RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.; RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of RT cystic fibrosis patients."; RL J. Bacteriol. 191:261-277(2009). 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 + NADPH + H(+); 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; AM747720; CAR52385.1; -; Genomic_DNA. DR RefSeq; WP_006483824.1; NC_011000.1. DR AlphaFoldDB; B4ECM5; -. DR SMR; B4ECM5; -. DR GeneID; 99783262; -. DR KEGG; bcj:BCAL2085; -. DR eggNOG; COG0743; Bacteria. DR HOGENOM; CLU_035714_4_0_4; -. DR BioCyc; BCEN216591:G1G1V-2285-MONOMER; -. DR UniPathway; UPA00056; UER00092. DR Proteomes; UP000001035; Chromosome 1. DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter. DR GO; GO:0070402; F:NADPH binding; IEA:InterPro. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniRule. DR FunFam; 3.40.50.720:FF:000045; 1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1. 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 NCBIfam; NF003938; PRK05447.1-1; 1. DR NCBIfam; NF009114; PRK12464.1; 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..398 FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase" FT /id="PRO_1000098477" FT BINDING 11 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 12 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 13 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 14 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 38 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 39 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 125 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 126 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 127 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 151 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 152 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 153 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 153 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 179 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 202 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 208 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" 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 220 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="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 224 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 224 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" SQ SEQUENCE 398 AA; 41924 MW; F8E11B68AA2256C5 CRC64; MQKRLTLLGS TGSIGDSTLD VVARHPERFS VYALTAHRNG DKLVEQCLRF APEVAVVGDA ATAAHVDAKL RAAGSKTVVL HGPQALVDVS KSDGCDTVVA AIVGAAGLAP SLAAARAGKR ILLANKEALV MSGAIFMDAV RDHGAILLPV DSEHNAIFQC MPRDAAEHGG ISKIILTASG GPFRTREPAT LVDVTPDEAC KHPNWVMGRK ISVDSATMMN KGLEVIEAHW IFGLPGDRID VLIHPQSVIH SLVSYRDGSV LAQLGNPDMR TPIAHALAFP ERVDAGVDQL DLAQIAQLSF EKPDYARFPC LALALKALEE GGIASAALNA ANEVAVEAFL ERRIGFMAIA ATVDAVLNTL PNRAPDGLDD VLAADAEARR LAAAIIAKAP APRVERTV //