Isopentenyl-diphosphate Delta-isomerase (Q46822)

Identification
Name:Isopentenyl-diphosphate Delta-isomerase
Synonyms:
  • IPP isomerase
  • IPP:DMAPP isomerase
  • Isopentenyl pyrophosphate isomerase
Gene Name:idi
Enzyme Class:
Biological Properties
General Function:Involved in isopentenyl-diphosphate delta-isomerase activity
Specific Function:Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)
Cellular Location:Cytoplasm
SMPDB Pathways:
  • Secondary metabolites: isoprenoid biosynthesis (nonmevalonate pathway) PW000975
  • Secondary metabolites: methylerythritol phosphate and polyisoprenoid biosynthesis PW000958
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb
1.0Isopentenyl pyrophosphate ↔ 1.0Dimethylallylpyrophosphate
ReactionCard
SMPDB Reactions:
1.0Isopentenyl pyrophosphate+1.0Thumb ↔ 1.0Dimethylallylpyrophosphate+1.0Thumb
1.0Isopentenyl pyrophosphate + 1.0Isopentenyl pyrophosphate ↔ 1.0Dimethylallylpyrophosphate + 1.0Dimethylallylpyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb
1.0Isopentenyl pyrophosphate ↔ 1.0Dimethylallylpyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb
1.0Isopentenyl pyrophosphate → 1.0Dimethylallylpyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01120DimethylallylpyrophosphateMetaboCard
ECMDB01347Isopentenyl pyrophosphateMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, transposing C=C bonds
isomerase activity
isopentenyl-diphosphate delta-isomerase activity
Process
cellular lipid metabolic process
isoprenoid biosynthetic process
isoprenoid metabolic process
lipid metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b2889
Gene OrientationClockwise
Centisome Percentage:65.33
Left Sequence End3031087
Right Sequence End3031635
Gene Sequence:
>549 bp
ATGCAAACGGAACACGTCATTTTATTGAATGCACAGGGAGTTCCCACGGGTACGCTGGAA
AAGTATGCCGCACACACGGCAGACACCCGCTTACATCTCGCGTTCTCCAGTTGGCTGTTT
AATGCCAAAGGACAATTATTAGTTACCCGCCGCGCACTGAGCAAAAAAGCATGGCCTGGC
GTGTGGACTAACTCGGTTTGTGGGCACCCACAACTGGGAGAAAGCAACGAAGACGCAGTG
ATCCGCCGTTGCCGTTATGAGCTTGGCGTGGAAATTACGCCTCCTGAATCTATCTATCCT
GACTTTCGCTACCGCGCCACCGATCCGAGTGGCATTGTGGAAAATGAAGTGTGTCCGGTA
TTTGCCGCACGCACCACTAGTGCGTTACAGATCAATGATGATGAAGTGATGGATTATCAA
TGGTGTGATTTAGCAGATGTATTACACGGTATTGATGCCACGCCGTGGGCGTTCAGTCCG
TGGATGGTGATGCAGGCGACAAATCGCGAAGCCAGAAAACGATTATCTGCATTTACCCAG
CTTAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:182
Protein Molecular Weight:20508
Protein Theoretical pI:6
PDB File:1PVF
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Isopentenyl-diphosphate Delta-isomerase
MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPG
VWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDPSGIVENEVCPV
FAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVMQATNREARKRLSAFTQ
LK
References
External Links:
ResourceLink
Uniprot ID:Q46822
Uniprot Name:IDI_ECOLI
GenBank Gene ID:AF119715
Genebank Protein ID:4633513
PDB ID:1PVF
Ecogene ID:EG13072
Ecocyc:EG13072
ColiBase:b2889
Kegg Gene:b2889
EchoBASE ID:EB2883
CCDB:IDI_ECOLI
BacMap:16130791
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bonanno, J. B., Edo, C., Eswar, N., Pieper, U., Romanowski, M. J., Ilyin, V., Gerchman, S. E., Kycia, H., Studier, F. W., Sali, A., Burley, S. K. (2001). "Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis." Proc Natl Acad Sci U S A 98:12896-12901. Pubmed: 11698677
  • de Ruyck, J., Durisotti, V., Oudjama, Y., Wouters, J. (2006). "Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography." J Biol Chem 281:17864-17869. Pubmed: 16617181
  • Durbecq, V., Sainz, G., Oudjama, Y., Clantin, B., Bompard-Gilles, C., Tricot, C., Caillet, J., Stalon, V., Droogmans, L., Villeret, V. (2001). "Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase." EMBO J 20:1530-1537. Pubmed: 11285217
  • Hahn, F. M., Hurlburt, A. P., Poulter, C. D. (1999). "Escherichia coli open reading frame 696 is idi, a nonessential gene encoding isopentenyl diphosphate isomerase." J Bacteriol 181:4499-4504. Pubmed: 10419945
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hemmi, H., Ohnuma, S., Nagaoka, K., Nishino, T. (1998). "Identification of genes affecting lycopene formation in Escherichia coli transformed with carotenoid biosynthetic genes: candidates for early genes in isoprenoid biosynthesis." J Biochem 123:1088-1096. Pubmed: 9603997
  • Wang, C. W., Oh, M. K., Liao, J. C. (1999). "Engineered isoprenoid pathway enhances astaxanthin production in Escherichia coli." Biotechnol Bioeng 62:235-241. Pubmed: 10099534
  • Wouters, J., Oudjama, Y., Barkley, S. J., Tricot, C., Stalon, V., Droogmans, L., Poulter, C. D. (2003). "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 278:11903-11908. Pubmed: 12540835
  • Wouters, J., Oudjama, Y., Ghosh, S., Stalon, V., Droogmans, L., Oldfield, E. (2003). "Structure and mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase." J Am Chem Soc 125:3198-3199. Pubmed: 12630859
  • Wouters, J., Oudjama, Y., Stalon, V., Droogmans, L., Poulter, C. D. (2004). "Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor." Proteins 54:216-221. Pubmed: 14696183
  • Wouters, J., Yin, F., Song, Y., Zhang, Y., Oudjama, Y., Stalon, V., Droogmans, L., Morita, C. T., Oldfield, E. (2005). "A crystallographic investigation of phosphoantigen binding to isopentenyl pyrophosphate/dimethylallyl pyrophosphate isomerase." J Am Chem Soc 127:536-537. Pubmed: 15643873