Identification
Name:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
Synonyms:
  • 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
  • Protein gcpE
  • Protein E
Gene Name:ispG
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate
Cellular Location:Not Available
SMPDB Pathways:
  • Secondary metabolites: isoprenoid biosynthesis (nonmevalonate pathway) PW000975
  • Secondary metabolites: methylerythritol phosphate and polyisoprenoid biosynthesis PW000958
KEGG Pathways:
KEGG Reactions:
1.0Thumb+2.0Reduced ferredoxin+1.0Oxidized ferredoxin1.0Thumb+1.0Thumb+2.0Oxidized ferredoxin+1.0Reduced ferredoxin
1.02-C-Methyl-D-erythritol-2,4-cyclodiphosphate + 2.0Reduced ferredoxin + 1.0Oxidized ferredoxin ↔ 1.01-Hydroxy-2-methyl-2-butenyl 4-diphosphate + 1.0Water + 2.0Oxidized ferredoxin + 1.0Reduced ferredoxin
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0a reduced flavodoxin1.0Thumb+1.0Thumb+1.0an oxidized flavodoxin+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Oxidized-ferredoxins1.0Thumb+1.0Thumb+1.0Reduced-ferredoxins
Complex Reactions:
1.0Thumb+2.0Flavodoxin reduced+1.0Thumb2.0flavodoxin semi oxidized+1.0Thumb+1.0Thumb
1.02-C-Methyl-D-erythritol-2,4-cyclodiphosphate + 2.0Flavodoxin reduced + 1.0Hydrogen ion → 2.0flavodoxin semi oxidized + 1.01-Hydroxy-2-methyl-2-butenyl 4-diphosphate + 1.0Water
ReactionCard
1.0Thumb+1.0Thumb+2.0oxidized ferredoxin1.0Thumb+2.0reduced ferredoxin
Metabolites:
ECMDB IDNameView
ECMDB214731-Hydroxy-2-methyl-2-(E)-butenyl 4-diphosphateMetaboCard
ECMDB200201-Hydroxy-2-methyl-2-butenyl 4-diphosphateMetaboCard
ECMDB231122-C-Methyl-D-erythritol 2,4-cyclodiphosphateMetaboCard
ECMDB041032-C-Methyl-D-erythritol-2,4-cyclodiphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity
binding
catalytic activity
cation binding
ion binding
iron ion binding
metal ion binding
oxidoreductase activity
oxidoreductase activity, acting on CH or CH2 groups
oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor
transition metal ion binding
Process
cellular lipid metabolic process
cellular metabolic process
isoprenoid biosynthetic process
isoprenoid metabolic process
lipid metabolic process
metabolic process
oxidation reduction
primary metabolic process
terpenoid biosynthetic process
terpenoid metabolic process
Gene Properties
Blattner:b2515
Gene OrientationCounterclockwise
Centisome Percentage:56.87
Left Sequence End2638708
Right Sequence End2639826
Gene Sequence:
>1119 bp
ATGAGCCTGCCTTTTTTACGCACGCTGCAAGGCGATCGTTTTTTTCAGTTATTAATTCTT
GTTGGTATCGGATTAAGCTTTTTCGTGCCCTTTGCACCGAAATCCTGGCCTGCTGCTATC
GACTGGCACACCATCATCACCTTAAGCGGCCTGATGCTGCTGACCAAAGGTGTGGAGTTA
AGCGGTTATTTTGATGTGCTGGGGCGCAAAATGGTGCGCCGCTTTGCTACGGAGCGTCGG
CTGGCGATGTTTATGGTGCTGGCGGCGGCGCTGCTTTCTACCTTTCTGACCAACGATGTC
GCGCTGTTTATTGTTGTTCCGCTGACTATCACGCTAAAAAGACTGTGTGAGATCCCGGTT
AATCGGCTGATTATTTTTGAGGCGCTGGCAGTCAACGCTGGTTCGCTACTGACGCCAATT
GGCAACCCGCAAAATATTCTTATCTGGGGACGTTCTGGTCTTTCGTTTGCCGGATTTATT
GCCCAAATGGCACCGCTGGCTGGCGCAATGATGCTGACGCTCCTGCTCCTGTGCTGGTGT
TGTTTCCCTGGAAAGGCGATGCAATACCATACGGGGGTGCAAACACCGGAGTGGAAACCG
CGGCTGGTGTGGAGTTGTCTGGGGCTGTATATCGTCTTTCTGACGGCGCTGGAGTTCAAA
CAAGAGCTGTGGGGACTGGTGATTGTGGCGGCAGGCTTTGCGCTGCTGGCACGTCGCGTG
GTGCTCAGTGTGGACTGGACGCTGCTGCTGGTGTTTATGGCGATGTTTATCGACGTCCAT
TTACTGACCCAGCTTCCAGCGTTGCAAGGCGTGTTGGGTAACGTGAGTCATCTATCTGAA
CCCGGGTTATGGTTAACGGCAATCGGTTTATCGCAGGTGATCAGTAACGTGCCGAGTACC
ATATTGTTGCTGAACTATGTGCCGCCGTCTTTATTACTGGTATGGGCGGTAAACGTAGGT
GGCTTTGGGTTATTACCCGGATCGCTGGCAAATTTGATTGCGCTACGTATGGCGAACGAT
CGCCGCATCTGGTGGCGTTTCCATCTCTATTCAATACCGATGCTGTTGTGGGCGGCGTTG
GTGGGATATGTTTTGTTAGTTATACTCCCGGCCAACTAG
Protein Properties
Pfam Domain Function:
Protein Residues:372
Protein Molecular Weight:40683
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
MHNQAPIQRRKSTRIYVGNVPIGDGAPIAVQSMTNTRTTDVEATVNQIKALERVGADIVR
VSVPTMDAAEAFKLIKQQVNVPLVADIHFDYRIALKVAEYGVDCLRINPGNIGNEERIRM
VVDCARDKNIPIRIGVNAGSLEKDLQEKYGEPTPQALLESAMRHVDHLDRLNFDQFKVSV
KASDVFLAVESYRLLAKQIDQPLHLGITEAGGARSGAVKSAIGLGLLLSEGIGDTLRVSL
AADPVEEIKVGFDILKSLRIRSRGINFIACPTCSRQEFDVIGTVNALEQRLEDIITPMDV
SIIGCVVNGPGEALVSTLGVTGGNKKSGLYEDGVRKDRLDNNDMIDQLEARIRAKASQLD
EARRIDVQQVEK
References
External Links:
ResourceLink
Uniprot ID:P62620
Uniprot Name:ISPG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062385
Ecogene ID:EG10370
Ecocyc:EG10370
ColiBase:b2515
Kegg Gene:b2515
EchoBASE ID:EB0365
CCDB:ISPG_ECOLI
BacMap:16130440
General Reference:
  • Altincicek, B., Kollas, A. K., Sanderbrand, S., Wiesner, J., Hintz, M., Beck, E., Jomaa, H. (2001). "GcpE is involved in the 2-C-methyl-D-erythritol 4-phosphate pathway of isoprenoid biosynthesis in Escherichia coli." J Bacteriol 183:2411-2416. Pubmed: 11274098
  • Baker, J., Franklin, D. B., Parker, J. (1992). "Sequence and characterization of the gcpE gene of Escherichia coli." FEMS Microbiol Lett 73:175-180. Pubmed: 1521767
  • 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
  • Campos, N., Rodriguez-Concepcion, M., Seemann, M., Rohmer, M., Boronat, A. (2001). "Identification of gcpE as a novel gene of the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis in Escherichia coli." FEBS Lett 488:170-173. Pubmed: 11163766
  • Freedman, R., Gibson, B., Donovan, D., Biemann, K., Eisenbeis, S., Parker, J., Schimmel, P. (1985). "Primary structure of histidine-tRNA synthetase and characterization of hisS transcripts." J Biol Chem 260:10063-10068. Pubmed: 2991272
  • 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
  • Hecht, S., Eisenreich, W., Adam, P., Amslinger, S., Kis, K., Bacher, A., Arigoni, D., Rohdich, F. (2001). "Studies on the nonmevalonate pathway to terpenes: the role of the GcpE (IspG) protein." Proc Natl Acad Sci U S A 98:14837-14842. Pubmed: 11752431
  • Rohdich, F., Zepeck, F., Adam, P., Hecht, S., Kaiser, J., Laupitz, R., Grawert, T., Amslinger, S., Eisenreich, W., Bacher, A., Arigoni, D. (2003). "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 100:1586-1591. Pubmed: 12571359
  • Sauret-Gueto, S., Ramos-Valdivia, A., Ibanez, E., Boronat, A., Rodriguez-Concepcion, M. (2003). "Identification of lethal mutations in Escherichia coli genes encoding enzymes of the methylerythritol phosphate pathway." Biochem Biophys Res Commun 307:408-415. Pubmed: 12859972
  • Seemann, M., Bui, B. T., Wolff, M., Tritsch, D., Campos, N., Boronat, A., Marquet, A., Rohmer, M. (2002). "Isoprenoid biosynthesis through the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE) is a [4Fe-4S] protein." Angew Chem Int Ed Engl 41:4337-4339. Pubmed: 12434382
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837