ID DXR_ECOLI Reviewed; 398 AA. AC P45568; P77209; Q8KMY5; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 194. DE RecName: Full=1-deoxy-D-xylulose 5-phosphate reductoisomerase; DE Short=DXP reductoisomerase; DE EC=1.1.1.267 {ECO:0000269|PubMed:10631325, ECO:0000269|PubMed:10787409, ECO:0000269|PubMed:9707569}; DE AltName: Full=1-deoxyxylulose-5-phosphate reductoisomerase; DE AltName: Full=2-C-methyl-D-erythritol 4-phosphate synthase; GN Name=dxr; Synonyms=ispC, yaeM; OrderedLocusNames=b0173, JW0168; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP PATHWAY. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9707569; DOI=10.1073/pnas.95.17.9879; RA Takahashi S., Kuzuyama T., Watanabe H., Seto H.; RT "A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation RT of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate RT pathway for terpenoid biosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9879-9884(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 RT - 6.0 min (189,987 - 281,416bp) region."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO RP 277-284. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-204. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8202364; DOI=10.1093/nar/22.9.1637; RA Fujita N., Mori H., Yura T., Ishihama A.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4- RT 4.1 min (110,917-193,643 bp) region."; RL Nucleic Acids Res. 22:1637-1639(1994). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49. RX PubMed=1447125; DOI=10.1128/jb.174.23.7517-7526.1992; RA Yamanaka K., Ogura T., Niki H., Hiraga S.; RT "Identification and characterization of the smbA gene, a suppressor of the RT mukB null mutant of Escherichia coli."; RL J. Bacteriol. 174:7517-7526(1992). RN [8] RP IDENTIFICATION. RX PubMed=7567469; DOI=10.1093/nar/23.17.3554; RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.; RT "Detection of new genes in a bacterial genome using Markov models for three RT gene classes."; RL Nucleic Acids Res. 23:3554-3562(1995). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10631325; DOI=10.1016/s0014-5793(99)01743-3; RA Radykewicz T., Rohdich F., Wungsintaweekul J., Herz S., Kis K., RA Eisenreich W., Bacher A., Zenk M.H., Arigoni D.; RT "Biosynthesis of terpenoids: 1-deoxy-D-xylulose-5-phosphate RT reductoisomerase from Escherichia coli is a class B dehydrogenase."; RL FEBS Lett. 465:157-160(2000). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND RP MUTAGENESIS OF GLY-14; HIS-153; HIS-209; GLU-231 AND HIS-257. RX PubMed=10787409; DOI=10.1074/jbc.m001820200; RA Kuzuyama T., Takahashi S., Takagi M., Seto H.; RT "Characterization of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an RT enzyme involved in isopentenyl diphosphate biosynthesis, and identification RT of its catalytic amino acid residues."; RL J. Biol. Chem. 275:19928-19932(2000). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-398 IN COMPLEX WITH NADPH. RX PubMed=11872159; DOI=10.1093/oxfordjournals.jbchem.a003105; RA Yajima S., Nonaka T., Kuzuyama T., Seto H., Ohsawa K.; RT "Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase RT complexed with cofactors: implications of a flexible loop movement upon RT substrate binding."; RL J. Biochem. 131:313-317(2002). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT. RX PubMed=11741911; DOI=10.1074/jbc.m109500200; RA Reuter K., Sanderbrand S., Jomaa H., Wiesner J., Steinbrecher I., Beck E., RA Hintz M., Klebe G., Stubbs M.T.; RT "Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a RT crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis."; RL J. Biol. Chem. 277:5378-5384(2002). RN [13] {ECO:0007744|PDB:1ONN, ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND RP FOSMIDOMYCIN, AND SUBUNIT. RX PubMed=12621040; DOI=10.1074/jbc.m300993200; RA Steinbacher S., Kaiser J., Eisenreich W., Huber R., Bacher A., Rohdich F.; RT "Structural basis of fosmidomycin action revealed by the complex with 2-C- RT methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the RT catalytic mechanism and anti-malaria drug development."; RL J. Biol. Chem. 278:18401-18407(2003). RN [14] {ECO:0007744|PDB:1T1R, ECO:0007744|PDB:1T1S} RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-398 IN COMPLEX WITH SUBSTRATE RP ANALOG. RX PubMed=15339150; DOI=10.1021/ja040126m; RA Yajima S., Hara K., Sanders J.M., Yin F., Ohsawa K., Wiesner J., Jomaa H., RA Oldfield E.; RT "Crystallographic structures of two bisphosphonate:1-deoxyxylulose-5- RT phosphate reductoisomerase complexes."; RL J. Am. Chem. Soc. 126:10824-10825(2004). RN [15] {ECO:0007744|PDB:1Q0H, ECO:0007744|PDB:1Q0L, ECO:0007744|PDB:1Q0Q} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH 1-DEOXY-D-XYLULOSE RP 5-PHOSPHATE; FOSMIDOMYCIN AND NADPH, AND SUBUNIT. RX PubMed=15567415; DOI=10.1016/j.jmb.2004.10.030; RA Mac Sweeney A., Lange R., Fernandes R.P., Schulz H., Dale G.E., RA Douangamath A., Proteau P.J., Oefner C.; RT "The crystal structure of E.coli 1-deoxy-D-xylulose-5-phosphate RT reductoisomerase in a ternary complex with the antimalarial compound RT fosmidomycin and NADPH reveals a tight-binding closed enzyme RT conformation."; RL J. Mol. Biol. 345:115-127(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:0000269|PubMed:10631325, CC ECO:0000269|PubMed:10787409, ECO:0000269|PubMed:9707569}. 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:0000269|PubMed:10631325, ECO:0000269|PubMed:10787409, CC ECO:0000269|PubMed:9707569}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13719; CC Evidence={ECO:0000269|PubMed:10631325, ECO:0000269|PubMed:10787409, CC ECO:0000269|PubMed:9707569}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10787409}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:10787409}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:10787409}; CC Note=Divalent cation. Prefers Mg(2+), Mn(2+) or Co(2+). CC {ECO:0000269|PubMed:10787409}; CC -!- ACTIVITY REGULATION: Inhibited by fosmidomycin. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=250 uM for DXP {ECO:0000269|PubMed:10787409}; CC Note=Measured in the presence of manganese ions.; CC pH dependence: CC Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:10787409}; CC Temperature dependence: CC Optimum temperature is 40-60 degrees Celsius. CC {ECO:0000269|PubMed:10787409}; 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:0000269|PubMed:9707569}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11741911, CC ECO:0000269|PubMed:11872159, ECO:0000269|PubMed:12621040, CC ECO:0000269|PubMed:15339150, ECO:0000269|PubMed:15567415}. CC -!- SIMILARITY: Belongs to the DXR family. {ECO:0000305}. 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; AB013300; BAA32426.1; -; Genomic_DNA. DR EMBL; U70214; AAB08602.1; -; Genomic_DNA. DR EMBL; U00096; AAC73284.1; -; Genomic_DNA. DR EMBL; AP009048; BAA77848.2; -; Genomic_DNA. DR EMBL; D13334; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; E64741; E64741. DR RefSeq; NP_414715.1; NC_000913.3. DR RefSeq; WP_000811923.1; NZ_CP009789.1. DR PDB; 1JVS; X-ray; 2.20 A; A/B=2-398. DR PDB; 1K5H; X-ray; 2.50 A; A/B/C=1-398. DR PDB; 1ONN; X-ray; 2.60 A; A/B=1-398. DR PDB; 1ONO; X-ray; 2.50 A; A/B=1-398. DR PDB; 1ONP; X-ray; 2.50 A; A/B=1-398. DR PDB; 1Q0H; X-ray; 2.20 A; A=1-398. DR PDB; 1Q0L; X-ray; 2.65 A; A=1-398. DR PDB; 1Q0Q; X-ray; 1.90 A; A/B=1-398. DR PDB; 1T1R; X-ray; 2.30 A; A/B=2-398. DR PDB; 1T1S; X-ray; 2.40 A; A/B=2-398. DR PDB; 2EGH; X-ray; 2.20 A; A/B=2-398. DR PDB; 3ANL; X-ray; 2.10 A; A/B=2-398. DR PDB; 3ANM; X-ray; 2.00 A; A/B=2-398. DR PDB; 3ANN; X-ray; 2.00 A; A/B=2-398. DR PDB; 3R0I; X-ray; 2.10 A; A/B=1-398. DR AlphaFoldDB; P45568; -. DR MDRepo; P45568; -. DR SMR; P45568; -. DR BioGRID; 4259751; 208. DR ComplexPortal; CPX-1930; DXP reductoisomerase complex. DR DIP; DIP-9484N; -. DR FunCoup; P45568; 471. DR IntAct; P45568; 6. DR STRING; 511145.b0173; -. DR BindingDB; P45568; -. DR ChEMBL; CHEMBL4091; -. DR DrugBank; DB02496; 1-Deoxy-D-xylulose 5-phosphate. DR DrugBank; DB03649; [{(5-Chloro-2-Pyridinyl)Amino} Methylene]-1,1-Bisphosphonate. DR DrugBank; DB02948; Fosmidomycin. DR jPOST; P45568; -. DR PaxDb; 511145-b0173; -. DR EnsemblBacteria; AAC73284; AAC73284; b0173. DR GeneID; 93777252; -. DR GeneID; 945019; -. DR KEGG; ecj:JW0168; -. DR KEGG; eco:b0173; -. DR KEGG; ecoc:C3026_00790; -. DR PATRIC; fig|1411691.4.peg.2107; -. DR EchoBASE; EB2575; -. DR eggNOG; COG0743; Bacteria. DR HOGENOM; CLU_035714_4_0_6; -. DR InParanoid; P45568; -. DR OMA; AHPNWVM; -. DR OrthoDB; 9806546at2; -. DR PhylomeDB; P45568; -. DR BioCyc; EcoCyc:DXPREDISOM-MONOMER; -. DR BioCyc; MetaCyc:DXPREDISOM-MONOMER; -. DR BRENDA; 1.1.1.267; 2026. DR SABIO-RK; P45568; -. DR UniPathway; UPA00056; UER00092. DR EvolutionaryTrace; P45568; -. DR PRO; PR:P45568; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:1990065; C:Dxr protein complex; IPI:ComplexPortal. DR GO; GO:0030604; F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc. DR GO; GO:0030145; F:manganese ion binding; IDA:EcoCyc. DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IDA:ComplexPortal. DR FunFam; 1.10.1740.10:FF:000004; 1-deoxy-D-xylulose 5-phosphate reductoisomerase; 1. 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. DR PDBsum; 1JVS; -. DR PDBsum; 1K5H; -. DR PDBsum; 1ONN; -. DR PDBsum; 1ONO; -. DR PDBsum; 1ONP; -. DR PDBsum; 1Q0H; -. DR PDBsum; 1Q0L; -. DR PDBsum; 1Q0Q; -. DR PDBsum; 1T1R; -. DR PDBsum; 1T1S; -. DR PDBsum; 2EGH; -. DR PDBsum; 3ANL; -. DR PDBsum; 3ANM; -. DR PDBsum; 3ANN; -. DR PDBsum; 3R0I; -. PE 1: Evidence at protein level; KW 3D-structure; Cobalt; Isoprene biosynthesis; Magnesium; Manganese; KW Metal-binding; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..398 FT /note="1-deoxy-D-xylulose 5-phosphate reductoisomerase" FT /id="PRO_0000163651" FT BINDING 10 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 11 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 12 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 13 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 36 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 37 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 38 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 124 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 125 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 126 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 150 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12621040, FT ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP" FT BINDING 151 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 152 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 152 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12621040, FT ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP" FT BINDING 186 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 209 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 215 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 222 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 227 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 228 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 231 FT /ligand="1-deoxy-D-xylulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:57792" FT /evidence="ECO:0000269|PubMed:15567415, FT ECO:0007744|PDB:1Q0Q" FT BINDING 231 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:12621040, FT ECO:0007744|PDB:1ONO, ECO:0007744|PDB:1ONP" FT MUTAGEN 14 FT /note="G->D: Loss of solubility and activity." FT /evidence="ECO:0000269|PubMed:10787409" FT MUTAGEN 153 FT /note="H->Q: Increase in KM for substrate. Reduces activity FT 35-fold." FT /evidence="ECO:0000269|PubMed:10787409" FT MUTAGEN 209 FT /note="H->Q: Increase in KM for substrate. Reduces activity FT 5000-fold." FT /evidence="ECO:0000269|PubMed:10787409" FT MUTAGEN 231 FT /note="E->K: No effect on KM for substrate. Reduces FT activity by over 99.9%." FT /evidence="ECO:0000269|PubMed:10787409" FT MUTAGEN 257 FT /note="H->Q: Strong increase in KM for substrate. Loss of FT activity." FT /evidence="ECO:0000269|PubMed:10787409" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:1Q0Q" FT TURN 8..10 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 12..23 FT /evidence="ECO:0007829|PDB:1Q0Q" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 28..37 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 59..71 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 82..89 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 107..115 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 119..122 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 125..131 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 133..142 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 151..158 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:1Q0Q" FT TURN 166..170 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 178..185 FT /evidence="ECO:0007829|PDB:1Q0Q" FT TURN 189..192 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 195..200 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 203..207 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:1JVS" FT HELIX 216..224 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 226..239 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 243..245 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 246..250 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 256..262 FT /evidence="ECO:0007829|PDB:1Q0Q" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 277..285 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 294..297 FT /evidence="ECO:0007829|PDB:1Q0Q" FT TURN 299..301 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:3ANM" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 316..327 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 329..347 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 355..366 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 370..372 FT /evidence="ECO:0007829|PDB:1Q0Q" FT HELIX 375..395 FT /evidence="ECO:0007829|PDB:1Q0Q" SQ SEQUENCE 398 AA; 43388 MW; 8B532683A4FF1207 CRC64; MKQLTILGST GSIGCSTLDV VRHNPEHFRV VALVAGKNVT RMVEQCLEFS PRYAVMDDEA SAKLLKTMLQ QQGSRTEVLS GQQAACDMAA LEDVDQVMAA IVGAAGLLPT LAAIRAGKTI LLANKESLVT CGRLFMDAVK QSKAQLLPVD SEHNAIFQSL PQPIQHNLGY ADLEQNGVVS ILLTGSGGPF RETPLRDLAT MTPDQACRHP NWSMGRKISV DSATMMNKGL EYIEARWLFN ASASQMEVLI HPQSVIHSMV RYQDGSVLAQ LGEPDMRTPI AHTMAWPNRV NSGVKPLDFC KLSALTFAAP DYDRYPCLKL AMEAFEQGQA ATTALNAANE ITVAAFLAQQ IRFTDIAALN LSVLEKMDMR EPQCVDDVLS VDANAREVAR KEVMRLAS //