4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Details
- Name
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Synonyms
- 1.17.1.2
- lytB
- yaaE
- Gene Name
- ispH
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0019513|4-hydroxy-3-methylbut-2-enyl diphosphate reductase MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQI SEVPDGAILIFSAHGVSQAVRNEAKSRDLTVFDATCPLVTKVHMEVARASRRGEESILIG HAGHPEVEGTMGQYSNPEGGMYLVESPDDVWKLTVKNEEKLSFMTQTTLSVDDTSDVIDA LRKRFPKIVGPRKDDICYATTNRQEAVRALAEQAEVVLVVGSKNSSNSNRLAELAQRMGK RAFLIDDAKDIQEEWVKEVKCVGVTAGASAPDILVQNVVARLQQLGGGEAIPLEGREENI VFEVPKELRVDIREVD
- Number of residues
- 316
- Molecular Weight
- 34774.275
- Theoretical pI
- 4.95
- GO Classification
- Functions3 iron, 4 sulfur cluster binding / 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity / hydroxymethylbutenyl pyrophosphate reductase activity / metal ion bindingProcessesdimethylallyl diphosphate biosynthetic process / isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway / terpenoid biosynthetic processComponentscytosol
- General Function
- Metal ion binding
- Specific Function
- Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is also involved in penicillin tolerance and control of the stringent response. Seems to directly or indirectly interact with RelA to maintain it in an inactive form during normal growth.
- Pfam Domain Function
- LYTB (PF02401)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0019514|4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH) ATGCAGATCCTGTTGGCCAACCCGCGTGGTTTTTGTGCCGGGGTAGACCGCGCTATCAGC ATTGTTGAAAACGCGCTGGCCATTTACGGCGCACCGATATATGTCCGTCACGAAGTGGTA CATAACCGCTATGTGGTCGATAGCTTGCGTGAGCGTGGGGCTATCTTTATTGAGCAGATT AGCGAAGTACCGGACGGCGCGATCCTGATTTTCTCCGCACACGGTGTTTCTCAGGCGGTA CGTAACGAAGCAAAAAGTCGCGATTTGACGGTGTTTGATGCCACCTGTCCGCTGGTGACC AAAGTGCATATGGAAGTCGCCCGCGCCAGTCGCCGTGGCGAAGAATCTATTCTCATCGGT CACGCCGGGCACCCGGAAGTGGAAGGGACAATGGGCCAGTACAGTAACCCGGAAGGGGGA ATGTATCTGGTCGAATCGCCGGACGATGTGTGGAAACTGACGGTCAAAAACGAAGAGAAG CTCTCCTTTATGACCCAGACCACGCTGTCGGTGGATGACACGTCTGATGTGATCGACGCG CTGCGTAAACGCTTCCCGAAAATTGTCGGTCCGCGCAAAGATGACATCTGCTACGCCACG ACTAACCGTCAGGAAGCGGTACGCGCCCTGGCAGAACAGGCGGAAGTTGTGTTGGTGGTC GGTTCGAAAAACTCCTCCAACTCCAACCGTCTGGCGGAGCTGGCCCAGCGTATGGGCAAA CGCGCGTTTTTGATTGACGATGCGAAAGACATCCAGGAAGAGTGGGTGAAAGAGGTTAAA TGCGTCGGCGTGACTGCGGGCGCATCGGCTCCGGATATTCTGGTGCAGAATGTGGTGGCA CGTTTGCAGCAGCTGGGCGGTGGTGAAGCCATTCCGCTGGAAGGCCGTGAAGAAAACATT GTTTTCGAAGTGCCGAAAGAGCTGCGTGTCGATATTCGTGAAGTCGATTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P62623 UniProtKB Entry Name ISPH_ECOLI GenBank Protein ID 18652795 GenBank Gene ID AY062212 - General References
- Rohdich F, Hecht S, Gartner K, Adam P, Krieger C, Amslinger S, Arigoni D, Bacher A, Eisenreich W: Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein. Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1158-63. Epub 2002 Jan 29. [Article]
- Bouvier J, Stragier P: Nucleotide sequence of the lsp-dapB interval in Escherichia coli. Nucleic Acids Res. 1991 Jan 11;19(1):180. [Article]
- Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [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]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Gustafson CE, Kaul S, Ishiguro EE: Identification of the Escherichia coli lytB gene, which is involved in penicillin tolerance and control of the stringent response. J Bacteriol. 1993 Feb;175(4):1203-5. [Article]
- Altincicek B, Kollas A, Eberl M, Wiesner J, Sanderbrand S, Hintz M, Beck E, Jomaa H: LytB, a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli. FEBS Lett. 2001 Jun 15;499(1-2):37-40. [Article]
- McAteer S, Coulson A, McLennan N, Masters M: The lytB gene of Escherichia coli is essential and specifies a product needed for isoprenoid biosynthesis. J Bacteriol. 2001 Dec;183(24):7403-7. [Article]
- Adam P, Hecht S, Eisenreich W, Kaiser J, Grawert T, Arigoni D, Bacher A, Rohdich F: Biosynthesis of terpenes: studies on 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12108-13. Epub 2002 Aug 27. [Article]
- Wolff M, Seemann M, Tse Sum Bui B, Frapart Y, Tritsch D, Garcia Estrabot A, Rodriguez-Concepcion M, Boronat A, Marquet A, Rohmer M: Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein. FEBS Lett. 2003 Apr 24;541(1-3):115-20. [Article]
- Rohdich F, Zepeck F, Adam P, Hecht S, Kaiser J, Laupitz R, Grawert T, Amslinger S, Eisenreich W, Bacher A, Arigoni D: The deoxyxylulose phosphate pathway of isoprenoid biosynthesis: studies on the mechanisms of the reactions catalyzed by IspG and IspH protein. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1586-91. Epub 2003 Feb 5. [Article]
- Grawert T, Kaiser J, Zepeck F, Laupitz R, Hecht S, Amslinger S, Schramek N, Schleicher E, Weber S, Haslbeck M, Buchner J, Rieder C, Arigoni D, Bacher A, Eisenreich W, Rohdich F: IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis. J Am Chem Soc. 2004 Oct 13;126(40):12847-55. [Article]
- Grawert T, Rohdich F, Span I, Bacher A, Eisenreich W, Eppinger J, Groll M: Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction. Angew Chem Int Ed Engl. 2009;48(31):5756-9. doi: 10.1002/anie.200900548. [Article]
- Grawert T, Span I, Eisenreich W, Rohdich F, Eppinger J, Bacher A, Groll M: Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1077-81. doi: 10.1073/pnas.0913045107. Epub 2009 Dec 28. [Article]
- Span I, Grawert T, Bacher A, Eisenreich W, Groll M: Crystal structures of mutant IspH proteins reveal a rotation of the substrate's hydroxymethyl group during catalysis. J Mol Biol. 2012 Feb 10;416(1):1-9. doi: 10.1016/j.jmb.2011.11.033. Epub 2011 Nov 23. [Article]