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
- Functionshydrolase activity / isopentenyl-diphosphate delta-isomerase activity / metal ion bindingProcessescellular response to DNA damage stimulus / dimethylallyl diphosphate biosynthetic process / isoprenoid biosynthetic processComponentscytoplasm
- 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
- NUDIX (PF00293)
- 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
Resource Link UniProtKB ID Q46822 UniProtKB Entry Name IDI_ECOLI GenBank Protein ID 4633513 GenBank Gene ID AF119715 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB01799 4-Hydroxy-3-Methyl Butyl Diphosphate experimental unknown Details DB02480 (S)-4-bromo-3-hydroxy-3-methylbutyl diphosphate experimental unknown Details DB03165 2-Dimethylamino-Ethyl-Diphosphate experimental unknown Details DB03366 Imidazole experimental, investigational unknown Details DB04170 4-bromo-3-hydroxy-3-methyl butyl diphosphate experimental unknown Details