ID DXR_CAMJR Reviewed; 356 AA. AC Q5HT65; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 02-SEP-2026, entry version 105. 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}; OrderedLocusNames=CJE1535; OS Campylobacter jejuni (strain RM1221). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=195099; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM1221; RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015; RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., RA Nelson K.E.; RT "Major structural differences and novel potential virulence mechanisms from RT the genomes of multiple Campylobacter species."; RL PLoS Biol. 3:72-85(2005). 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; CP000025; AAW35972.1; -; Genomic_DNA. DR RefSeq; WP_002867315.1; NC_003912.7. DR AlphaFoldDB; Q5HT65; -. DR SMR; Q5HT65; -. DR KEGG; cjr:CJE1535; -. DR HOGENOM; CLU_035714_4_0_7; -. DR UniPathway; UPA00056; UER00092. 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 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. FT CHAIN 1..356 FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase" FT /id="PRO_0000163627" FT BINDING 7 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 8 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 9 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 10 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 31 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 33 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 111 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 112 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 113 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 131 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 132 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 133 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 133 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 155 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 178 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 184 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 191 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 196 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 197 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 200 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" FT BINDING 200 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00183" SQ SEQUENCE 356 AA; 39518 MW; DCD9A1CBE305EAF8 CRC64; MILFGSTGSI GVNALKLAAL KNIPISALAC GDNIALLNEQ IARFKPKFVA IKDSKNKHLV KHDRVFIGQE GLEQILTECQ DKLLLNAIVG FAGLKSTLKA KELGKNIALA NKESLVVAGS FLKGAKFLPV DSEHAALKFL LEGKKNIAKL YITASGGAFY KYKIKDLNQV SLKDALKHPN WNMGAKITID SATMANKLFE IIEAYHLYDF KEIDALIEPR SLVHAMCEFK NGASTAYFSK ADMKLAISDA IFEKQDTPIL EAVDFSKMPA LKFHPISTKK YPIFKLKNTF LKEPNLGVII NAANEVGVYN FLENKSGFLD IAKCIFKALD HFGVPKISSI EEVFEYDFKT REYLRS //