Isopentenyl-diphosphate Delta-isomerase

NameIsopentenyl-diphosphate Delta-isomerase
Synonyms
  • 5.3.3.2
  • IPP isomerase
  • IPP:DMAPP isomerase
  • Isopentenyl pyrophosphate isomerase
  • ygfV
Gene Nameidi
OrganismEscherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0020531|Isopentenyl-diphosphate Delta-isomerase
MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPG
VWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDPSGIVENEVCPV
FAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVMQATNREARKRLSAFTQ
LK
Number of residues182
Molecular Weight20508.085
Theoretical pI6.35
GO Classification
Functions
  • hydrolase activity
  • metal ion binding
  • isopentenyl-diphosphate delta-isomerase activity
Processes
  • cellular response to DNA damage stimulus
  • isoprenoid biosynthetic process
  • dimethylallyl diphosphate biosynthetic process
Components
  • cytoplasm
General FunctionMetal ion binding
Specific FunctionCatalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID4633513
UniProtKB IDQ46822
UniProtKB Entry NameIDI_ECOLI
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0020532|Isopentenyl-diphosphate Delta-isomerase (idi)
ATGCAAACGGAACACGTCATTTTATTGAATGCACAGGGAGTTCCCACGGGTACGCTGGAA
AAGTATGCCGCACACACGGCAGACACCCGCTTACATCTCGCGTTCTCCAGTTGGCTGTTT
AATGCCAAAGGACAATTATTAGTTACCCGCCGCGCACTGAGCAAAAAAGCATGGCCTGGC
GTGTGGACTAACTCGGTTTGTGGGCACCCACAACTGGGAGAAAGCAACGAAGACGCAGTG
ATCCGCCGTTGCCGTTATGAGCTTGGCGTGGAAATTACGCCTCCTGAATCTATCTATCCT
GACTTTCGCTACCGCGCCACCGATCCGAGTGGCATTGTGGAAAATGAAGTGTGTCCGGTA
TTTGCCGCACGCACCACTAGTGCGTTACAGATCAATGATGATGAAGTGATGGATTATCAA
TGGTGTGATTTAGCAGATGTATTACACGGTATTGATGCCACGCCGTGGGCGTTCAGTCCG
TGGATGGTGATGCAGGCGACAAATCGCGAAGCCAGAAAACGATTATCTGCATTTACCCAG
CTTAAATAA
GenBank Gene IDAF119715
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
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. 10099534
  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. 9278503
  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. 16738553
  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. 9603997
  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. 10419945
  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. 11285217
  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. 11698677
  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. 12630859
  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. 12540835
  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. 14696183
  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. 15643873
  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. 16617181