Identification |
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Name | Farnesyl pyrophosphate synthase |
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Synonyms | - FPP synthase
- FPS
- Farnesyl diphosphate synthase
- Dimethylallyltranstransferase
- Geranyltranstransferase
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Gene Name | ERG20 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in isoprenoid biosynthetic process |
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Specific Function | Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate |
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Cellular Location | Cytoplasm |
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SMPDB Pathways | Cholesterol biosynthesis and metabolism CE(10:0) | PW002545 | | Cholesterol biosynthesis and metabolism CE(12:0) | PW002548 | | Cholesterol biosynthesis and metabolism CE(14:0) | PW002544 | | Cholesterol biosynthesis and metabolism CE(16:0) | PW002550 | | Cholesterol biosynthesis and metabolism CE(18:0) | PW002551 | |
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KEGG Pathways | Terpenoid backbone biosynthesis | ec00900 | |
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SMPDB Reactions | |
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KEGG Reactions | |
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Metabolites | YMDB ID | Name | View |
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YMDB00095 | Dimethylallylpyrophosphate | Show | YMDB00200 | Isopentenyl pyrophosphate | Show | YMDB00219 | Pyrophosphate | Show | YMDB00229 | Farnesyl pyrophosphate | Show | YMDB00266 | Geranyl-PP | Show | YMDB00325 | 2-trans,6-trans-farnesyl diphosphate | Show | YMDB00670 | geranyl diphosphate | Show |
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GO Classification | Component |
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Not Available | Function |
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Not Available | Process |
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metabolic process | primary metabolic process | lipid metabolic process | cellular lipid metabolic process | isoprenoid metabolic process | isoprenoid biosynthetic process |
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Gene Properties |
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Chromosome Location | chromosome 10 |
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Locus | YJL167W |
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Gene Sequence | >1059 bp
ATGGCTTCAGAAAAAGAAATTAGGAGAGAGAGATTCTTGAACGTTTTCCCTAAATTAGTA
GAGGAATTGAACGCATCGCTTTTGGCTTACGGTATGCCTAAGGAAGCATGTGACTGGTAT
GCCCACTCATTGAACTACAACACTCCAGGCGGTAAGCTAAATAGAGGTTTGTCCGTTGTG
GACACGTATGCTATTCTCTCCAACAAGACCGTTGAACAATTGGGGCAAGAAGAATACGAA
AAGGTTGCCATTCTAGGTTGGTGCATTGAGTTGTTGCAGGCTTACTTCTTGGTCGCCGAT
GATATGATGGACAAGTCCATTACCAGAAGAGGCCAACCATGTTGGTACAAGGTTCCTGAA
GTTGGGGAAATTGCCATCAATGACGCATTCATGTTAGAGGCTGCTATCTACAAGCTTTTG
AAATCTCACTTCAGAAACGAAAAATACTACATAGATATCACCGAATTGTTCCATGAGGTC
ACCTTCCAAACCGAATTGGGCCAATTGATGGACTTAATCACTGCACCTGAAGACAAAGTC
GACTTGAGTAAGTTCTCCCTAAAGAAGCACTCCTTCATAGTTACTTTCAAGACTGCTTAC
TATTCTTTCTACTTGCCTGTCGCATTGGCCATGTACGTTGCCGGTATCACGGATGAAAAG
GATTTGAAACAAGCCAGAGATGTCTTGATTCCATTGGGTGAATACTTCCAAATTCAAGAT
GACTACTTAGACTGCTTCGGTACCCCAGAACAGATCGGTAAGATCGGTACAGATATCCAA
GATAACAAATGTTCTTGGGTAATCAACAAGGCATTGGAACTTGCTTCCGCAGAACAAAGA
AAGACTTTAGACGAAAATTACGGTAAGAAGGACTCAGTCGCAGAAGCCAAATGCAAAAAG
ATTTTCAATGACTTGAAAATTGAACAGCTATACCACGAATATGAAGAGTCTATTGCCAAG
GATTTGAAGGCCAAAATTTCTCAGGTCGATGAGTCTCGTGGCTTCAAAGCTGATGTCTTA
ACTGCGTTCTTGAACAAAGTTTACAAGAGAAGCAAATAG |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 352 |
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Protein Molecular Weight | 40483.0 |
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Protein Theoretical pI | 5.11 |
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Signalling Regions | |
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Transmembrane Regions | |
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Protein Sequence | >Farnesyl pyrophosphate synthase
MASEKEIRRERFLNVFPKLVEELNASLLAYGMPKEACDWYAHSLNYNTPGGKLNRGLSVV
DTYAILSNKTVEQLGQEEYEKVAILGWCIELLQAYFLVADDMMDKSITRRGQPCWYKVPE
VGEIAINDAFMLEAAIYKLLKSHFRNEKYYIDITELFHEVTFQTELGQLMDLITAPEDKV
DLSKFSLKKHSFIVTFKTAYYSFYLPVALAMYVAGITDEKDLKQARDVLIPLGEYFQIQD
DYLDCFGTPEQIGKIGTDIQDNKCSWVINKALELASAEQRKTLDENYGKKDSVAEAKCKK
IFNDLKIEQLYHEYEESIAKDLKAKISQVDESRGFKADVLTAFLNKVYKRSK |
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References |
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External Links | |
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General Reference | - Anderson, M. S., Yarger, J. G., Burck, C. L., Poulter, C. D. (1989). "Farnesyl diphosphate synthetase. Molecular cloning, sequence, and expression of an essential gene from Saccharomyces cerevisiae." J Biol Chem 264:19176-19184.2681213
- Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
- Maarse, A. C., Grivell, L. A. (1987). "Nucleotide sequence of the gene encoding the 11-kDa subunit of the ubiquinol-cytochrome-c oxidoreductase in Saccharomyces cerevisiae." Eur J Biochem 165:419-425.3036507
- Blanchard, L., Karst, F. (1993). "Characterization of a lysine-to-glutamic acid mutation in a conservative sequence of farnesyl diphosphate synthase from Saccharomyces cerevisiae." Gene 125:185-189.8096487
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