1-deoxy-D-xylulose 5-phosphate reductoisomerase (P45568)

Identification
Name:1-deoxy-D-xylulose 5-phosphate reductoisomerase
Synonyms:
  • DXP reductoisomerase
  • 1-deoxyxylulose-5-phosphate reductoisomerase
  • 2-C-methyl-D-erythritol 4-phosphate synthase
Gene Name:dxr
Enzyme Class:
Biological Properties
General Function:Involved in 1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
Specific Function:Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP)
Cellular Location:Not Available
SMPDB Pathways:
  • Secondary metabolites: isoprenoid biosynthesis (nonmevalonate pathway) PW000975
  • Secondary metabolites: methylerythritol phosphate and polyisoprenoid biosynthesis PW000958
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.01-Deoxy-D-xylulose 5-phosphate + 1.0Hydrogen ion + 1.0NADPH ↔ 1.02-C-Methyl-D-erythritol-4-phosphate + 1.0NADP
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.02-C-Methyl-D-erythritol-4-phosphate + 1.0NADP ↔ 1.01-Deoxy-D-xylulose 5-phosphate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0NADPH+1.0Thumb+1.01-Deoxy-D-xylulose 5-phosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.02-C-methyl-D-erythritol 4-phosphate
1.0NADPH + 1.0Hydrogen ion + 1.01-Deoxy-D-xylulose 5-phosphate + 1.0NADPH + 1.01-Deoxy-D-xylulose 5-phosphate → 1.0NADP + 1.02-C-methyl-D-erythritol 4-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.01-Deoxy-D-xylulose 5-phosphate + 1.0Hydrogen ion + 1.0NADPH ↔ 1.02-C-Methyl-D-erythritol-4-phosphate + 1.0NADP
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.02-C-Methyl-D-erythritol-4-phosphate + 1.0NADP ↔ 1.01-Deoxy-D-xylulose 5-phosphate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB012131-Deoxy-D-xylulose 5-phosphateMetaboCard
ECMDB041042-C-Methyl-D-erythritol-4-phosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
GO Classification:
Function
1-deoxy-D-xylulose-5-phosphate reductoisomerase activity
binding
catalytic activity
cation binding
ion binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
cellular lipid metabolic process
isoprenoid biosynthetic process
isoprenoid metabolic process
lipid metabolic process
metabolic process
oxidation reduction
primary metabolic process
Gene Properties
Blattner:b0173
Gene OrientationClockwise
Centisome Percentage:4.17
Left Sequence End193521
Right Sequence End194717
Gene Sequence:
>1197 bp
ATGAAGCAACTCACCATTCTGGGCTCGACCGGCTCGATTGGTTGCAGCACGCTGGACGTG
GTGCGCCATAATCCCGAACACTTCCGCGTAGTTGCGCTGGTGGCAGGCAAAAATGTCACT
CGCATGGTAGAACAGTGCCTGGAATTCTCTCCCCGCTATGCCGTAATGGACGATGAAGCG
AGTGCGAAACTTCTTAAAACGATGCTACAGCAACAGGGTAGCCGCACCGAAGTCTTAAGT
GGGCAACAAGCCGCTTGCGATATGGCAGCGCTTGAGGATGTTGATCAGGTGATGGCAGCC
ATTGTTGGCGCTGCTGGGCTGTTACCTACGCTTGCTGCGATCCGCGCGGGTAAAACCATT
TTGCTGGCCAATAAAGAATCACTGGTTACCTGCGGACGTCTGTTTATGGACGCCGTAAAG
CAGAGCAAAGCGCAATTGTTACCGGTCGATAGCGAACATAACGCCATTTTTCAGAGTTTA
CCGCAACCTATCCAGCATAATCTGGGATACGCTGACCTTGAGCAAAATGGCGTGGTGTCC
ATTTTACTTACCGGGTCTGGTGGCCCTTTCCGTGAGACGCCATTGCGCGATTTGGCAACA
ATGACGCCGGATCAAGCCTGCCGTCATCCGAACTGGTCGATGGGGCGTAAAATTTCTGTC
GATTCGGCTACCATGATGAACAAAGGTCTGGAATACATTGAAGCGCGTTGGCTGTTTAAC
GCCAGCGCCAGCCAGATGGAAGTGCTGATTCACCCGCAGTCAGTGATTCACTCAATGGTG
CGCTATCAGGACGGCAGTGTTCTGGCGCAGCTGGGGGAACCGGATATGCGTACGCCAATT
GCCCACACCATGGCATGGCCGAATCGCGTGAACTCTGGCGTGAAGCCGCTCGATTTTTGC
AAACTAAGTGCGTTGACATTTGCCGCACCGGATTATGATCGTTATCCATGCCTGAAACTG
GCGATGGAGGCGTTCGAACAAGGCCAGGCAGCGACGACAGCATTGAATGCCGCAAACGAA
ATCACCGTTGCTGCTTTTCTTGCGCAACAAATCCGCTTTACGGATATCGCTGCGTTGAAT
TTATCCGTACTGGAAAAAATGGATATGCGCGAACCACAATGTGTGGACGATGTGTTATCT
GTTGATGCGAACGCGCGTGAAGTCGCCAGAAAAGAGGTGATGCGTCTCGCAAGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:398
Protein Molecular Weight:43388
Protein Theoretical pI:6
PDB File:1ONP
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>1-deoxy-D-xylulose 5-phosphate reductoisomerase
MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEA
SAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTI
LLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVS
ILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN
ASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFC
KLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALN
LSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS
References
External Links:
ResourceLink
Uniprot ID:P45568
Uniprot Name:DXR_ECOLI
GenBank Gene ID:AB013300
Genebank Protein ID:3434984
PDB ID:1ONP
Ecogene ID:EG12715
Ecocyc:EG12715
ColiBase:b0173
Kegg Gene:b0173
EchoBASE ID:EB2575
CCDB:DXR_ECOLI
BacMap:16128166
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Borodovsky, M., McIninch, J. D., Koonin, E. V., Rudd, K. E., Medigue, C., Danchin, A. (1995). "Detection of new genes in a bacterial genome using Markov models for three gene classes." Nucleic Acids Res 23:3554-3562. Pubmed: 7567469
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kuzuyama, T., Takahashi, S., Takagi, M., Seto, H. (2000). "Characterization of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an enzyme involved in isopentenyl diphosphate biosynthesis, and identification of its catalytic amino acid residues." J Biol Chem 275:19928-19932. Pubmed: 10787409
  • Mac Sweeney, A., Lange, R., Fernandes, R. P., Schulz, H., Dale, G. E., Douangamath, A., Proteau, P. J., Oefner, C. (2005). "The crystal structure of E.coli 1-deoxy-D-xylulose-5-phosphate reductoisomerase in a ternary complex with the antimalarial compound fosmidomycin and NADPH reveals a tight-binding closed enzyme conformation." J Mol Biol 345:115-127. Pubmed: 15567415
  • Radykewicz, T., Rohdich, F., Wungsintaweekul, J., Herz, S., Kis, K., Eisenreich, W., Bacher, A., Zenk, M. H., Arigoni, D. (2000). "Biosynthesis of terpenoids: 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Escherichia coli is a class B dehydrogenase." FEBS Lett 465:157-160. Pubmed: 10631325
  • Reuter, K., Sanderbrand, S., Jomaa, H., Wiesner, J., Steinbrecher, I., Beck, E., Hintz, M., Klebe, G., Stubbs, M. T. (2002). "Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis." J Biol Chem 277:5378-5384. Pubmed: 11741911
  • Steinbacher, S., Kaiser, J., Eisenreich, W., Huber, R., Bacher, A., Rohdich, F. (2003). "Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the catalytic mechanism and anti-malaria drug development." J Biol Chem 278:18401-18407. Pubmed: 12621040
  • Takahashi, S., Kuzuyama, T., Watanabe, H., Seto, H. (1998). "A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis." Proc Natl Acad Sci U S A 95:9879-9884. Pubmed: 9707569
  • Yajima, S., Hara, K., Sanders, J. M., Yin, F., Ohsawa, K., Wiesner, J., Jomaa, H., Oldfield, E. (2004). "Crystallographic structures of two bisphosphonate:1-deoxyxylulose-5-phosphate reductoisomerase complexes." J Am Chem Soc 126:10824-10825. Pubmed: 15339150
  • Yajima, S., Nonaka, T., Kuzuyama, T., Seto, H., Ohsawa, K. (2002). "Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with cofactors: implications of a flexible loop movement upon substrate binding." J Biochem 131:313-317. Pubmed: 11872159
  • Yamanaka, K., Ogura, T., Niki, H., Hiraga, S. (1992). "Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli." J Bacteriol 174:7517-7526. Pubmed: 1447125