Isopentenyl-diphosphate Delta-isomerase

Details

Name
Isopentenyl-diphosphate Delta-isomerase
Synonyms
  • 5.3.3.2
  • IPP isomerase
  • IPP:DMAPP isomerase
  • Isopentenyl pyrophosphate isomerase
  • ygfV
Gene Name
idi
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020531|Isopentenyl-diphosphate Delta-isomerase
MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPG
VWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDPSGIVENEVCPV
FAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVMQATNREARKRLSAFTQ
LK
Number of residues
182
Molecular Weight
20508.085
Theoretical pI
6.35
GO Classification
Functions
hydrolase activity / isopentenyl-diphosphate delta-isomerase activity / metal ion binding
Processes
cellular response to DNA damage stimulus / dimethylallyl diphosphate biosynthetic process / isoprenoid biosynthetic process
Components
cytoplasm
General Function
Metal ion binding
Specific Function
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0020532|Isopentenyl-diphosphate Delta-isomerase (idi)
ATGCAAACGGAACACGTCATTTTATTGAATGCACAGGGAGTTCCCACGGGTACGCTGGAA
AAGTATGCCGCACACACGGCAGACACCCGCTTACATCTCGCGTTCTCCAGTTGGCTGTTT
AATGCCAAAGGACAATTATTAGTTACCCGCCGCGCACTGAGCAAAAAAGCATGGCCTGGC
GTGTGGACTAACTCGGTTTGTGGGCACCCACAACTGGGAGAAAGCAACGAAGACGCAGTG
ATCCGCCGTTGCCGTTATGAGCTTGGCGTGGAAATTACGCCTCCTGAATCTATCTATCCT
GACTTTCGCTACCGCGCCACCGATCCGAGTGGCATTGTGGAAAATGAAGTGTGTCCGGTA
TTTGCCGCACGCACCACTAGTGCGTTACAGATCAATGATGATGAAGTGATGGATTATCAA
TGGTGTGATTTAGCAGATGTATTACACGGTATTGATGCCACGCCGTGGGCGTTCAGTCCG
TGGATGGTGATGCAGGCGACAAATCGCGAAGCCAGAAAACGATTATCTGCATTTACCCAG
CTTAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ46822
UniProtKB Entry NameIDI_ECOLI
GenBank Protein ID4633513
GenBank Gene IDAF119715
General References
  1. Wang CW, Oh MK, Liao JC: Engineered isoprenoid pathway enhances astaxanthin production in Escherichia coli. Biotechnol Bioeng. 1999 Jan 20;62(2):235-41. [Article]
  2. 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]
  3. 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]
  4. Hemmi H, Ohnuma S, Nagaoka K, Nishino T: Identification of genes affecting lycopene formation in Escherichia coli transformed with carotenoid biosynthetic genes: candidates for early genes in isoprenoid biosynthesis. J Biochem. 1998 Jun;123(6):1088-96. [Article]
  5. Hahn FM, Hurlburt AP, Poulter CD: Escherichia coli open reading frame 696 is idi, a nonessential gene encoding isopentenyl diphosphate isomerase. J Bacteriol. 1999 Aug;181(15):4499-504. [Article]
  6. Durbecq V, Sainz G, Oudjama Y, Clantin B, Bompard-Gilles C, Tricot C, Caillet J, Stalon V, Droogmans L, Villeret V: Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase. EMBO J. 2001 Apr 2;20(7):1530-7. [Article]
  7. Bonanno JB, Edo C, Eswar N, Pieper U, Romanowski MJ, Ilyin V, Gerchman SE, Kycia H, Studier FW, Sali A, Burley SK: Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis. Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12896-901. [Article]
  8. Wouters J, Oudjama Y, Ghosh S, Stalon V, Droogmans L, Oldfield E: Structure and mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase. J Am Chem Soc. 2003 Mar 19;125(11):3198-9. [Article]
  9. Wouters J, Oudjama Y, Barkley SJ, Tricot C, Stalon V, Droogmans L, Poulter CD: Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors. J Biol Chem. 2003 Apr 4;278(14):11903-8. Epub 2003 Jan 22. [Article]
  10. Wouters J, Oudjama Y, Stalon V, Droogmans L, Poulter CD: Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor. Proteins. 2004 Feb 1;54(2):216-21. [Article]
  11. Wouters J, Yin F, Song Y, Zhang Y, Oudjama Y, Stalon V, Droogmans L, Morita CT, Oldfield E: A crystallographic investigation of phosphoantigen binding to isopentenyl pyrophosphate/dimethylallyl pyrophosphate isomerase. J Am Chem Soc. 2005 Jan 19;127(2):536-7. [Article]
  12. de Ruyck J, Durisotti V, Oudjama Y, Wouters J: Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography. J Biol Chem. 2006 Jun 30;281(26):17864-9. Epub 2006 Apr 15. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB017994-Hydroxy-3-Methyl Butyl DiphosphateexperimentalunknownDetails
DB02480(S)-4-bromo-3-hydroxy-3-methylbutyl diphosphateexperimentalunknownDetails
DB031652-Dimethylamino-Ethyl-DiphosphateexperimentalunknownDetails
DB03366Imidazoleexperimental, investigationalunknownDetails
DB041704-bromo-3-hydroxy-3-methyl butyl diphosphateexperimentalunknownDetails