1-deoxy-D-xylulose 5-phosphate reductoisomerase
Details
- Name
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Synonyms
- 1-deoxyxylulose-5-phosphate reductoisomerase
- 1.1.1.267
- 2-C-methyl-D-erythritol 4-phosphate synthase
- DXP reductoisomerase
- ispC
- yaeM
- Gene Name
- dxr
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011117|1-deoxy-D-xylulose 5-phosphate reductoisomerase MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEA SAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTI LLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVS ILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFN ASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFC KLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALN LSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS
- Number of residues
- 398
- Molecular Weight
- 43387.575
- Theoretical pI
- 5.88
- GO Classification
- Functions1-deoxy-D-xylulose-5-phosphate reductoisomerase activity / identical protein binding / manganese ion binding / metal ion binding / NADPH bindingProcessesisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway / isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway involved in terpenoid biosynthetic process
- General Function
- Nadph binding
- 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).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011118|1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr) ATGAAGCAACTCACCATTCTGGGCTCGACCGGCTCGATTGGTTGCAGCACGCTGGACGTG GTGCGCCATAATCCCGAACACTTCCGCGTAGTTGCGCTGGTGGCAGGCAAAAATGTCACT CGCATGGTAGAACAGTGCCTGGAATTCTCTCCCCGCTATGCCGTAATGGACGATGAAGCG AGTGCGAAACTTCTTAAAACGATGCTACAGCAACAGGGTAGCCGCACCGAAGTCTTAAGT GGGCAACAAGCCGCTTGCGATATGGCAGCGCTTGAGGATGTTGATCAGGTGATGGCAGCC ATTGTTGGCGCTGCTGGGCTGTTACCTACGCTTGCTGCGATCCGCGCGGGTAAAACCATT TTGCTGGCCAATAAAGAATCACTGGTTACCTGCGGACGTCTGTTTATGGACGCCGTAAAG CAGAGCAAAGCGCAATTGTTACCGGTCGATAGCGAACATAACGCCATTTTTCAGAGTTTA CCGCAACCTATCCAGCATAATCTGGGATACGCTGACCTTGAGCAAAATGGCGTGGTGTCC ATTTTACTTACCGGGTCTGGTGGCCCTTTCCGTGAGACGCCATTGCGCGATTTGGCAACA ATGACGCCGGATCAAGCCTGCCGTCATCCGAACTGGTCGATGGGGCGTAAAATTTCTGTC GATTCGGCTACCATGATGAACAAAGGTCTGGAATACATTGAAGCGCGTTGGCTGTTTAAC GCCAGCGCCAGCCAGATGGAAGTGCTGATTCACCCGCAGTCAGTGATTCACTCAATGGTG CGCTATCAGGACGGCAGTGTTCTGGCGCAGCTGGGGGAACCGGATATGCGTACGCCAATT GCCCACACCATGGCATGGCCGAATCGCGTGAACTCTGGCGTGAAGCCGCTCGATTTTTGC AAACTAAGTGCGTTGACATTTGCCGCACCGGATTATGATCGTTATCCATGCCTGAAACTG GCGATGGAGGCGTTCGAACAAGGCCAGGCAGCGACGACAGCATTGAATGCCGCAAACGAA ATCACCGTTGCTGCTTTTCTTGCGCAACAAATCCGCTTTACGGATATCGCTGCGTTGAAT TTATCCGTACTGGAAAAAATGGATATGCGCGAACCACAATGTGTGGACGATGTGTTATCT GTTGATGCGAACGCGCGTGAAGTCGCCAGAAAAGAGGTGATGCGTCTCGCAAGCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P45568 UniProtKB Entry Name DXR_ECOLI GenBank Protein ID 3434984 GenBank Gene ID AB013300 - General References
- Takahashi S, Kuzuyama T, Watanabe H, Seto H: 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. 1998 Aug 18;95(17):9879-84. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
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- Fujita N, Mori H, Yura T, Ishihama A: Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. 1994 May 11;22(9):1637-9. [Article]
- Yamanaka K, Ogura T, Niki H, Hiraga S: Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli. J Bacteriol. 1992 Dec;174(23):7517-26. [Article]
- Borodovsky M, McIninch JD, Koonin EV, Rudd KE, Medigue C, Danchin A: Detection of new genes in a bacterial genome using Markov models for three gene classes. Nucleic Acids Res. 1995 Sep 11;23(17):3554-62. [Article]
- Radykewicz T, Rohdich F, Wungsintaweekul J, Herz S, Kis K, Eisenreich W, Bacher A, Zenk MH, Arigoni D: Biosynthesis of terpenoids: 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Escherichia coli is a class B dehydrogenase. FEBS Lett. 2000 Jan 14;465(2-3):157-60. [Article]
- Kuzuyama T, Takahashi S, Takagi M, Seto H: 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. 2000 Jun 30;275(26):19928-32. [Article]
- Yajima S, Nonaka T, Kuzuyama T, Seto H, Ohsawa K: Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase complexed with cofactors: implications of a flexible loop movement upon substrate binding. J Biochem. 2002 Mar;131(3):313-7. [Article]
- Reuter K, Sanderbrand S, Jomaa H, Wiesner J, Steinbrecher I, Beck E, Hintz M, Klebe G, Stubbs MT: Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. J Biol Chem. 2002 Feb 15;277(7):5378-84. Epub 2001 Dec 7. [Article]
- Steinbacher S, Kaiser J, Eisenreich W, Huber R, Bacher A, Rohdich F: 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. 2003 May 16;278(20):18401-7. Epub 2003 Mar 5. [Article]
- Yajima S, Hara K, Sanders JM, Yin F, Ohsawa K, Wiesner J, Jomaa H, Oldfield E: Crystallographic structures of two bisphosphonate:1-deoxyxylulose-5-phosphate reductoisomerase complexes. J Am Chem Soc. 2004 Sep 8;126(35):10824-5. [Article]
- Mac Sweeney A, Lange R, Fernandes RP, Schulz H, Dale GE, Douangamath A, Proteau PJ, Oefner C: 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. 2005 Jan 7;345(1):115-27. [Article]