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P08524 (FPPS_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Farnesyl pyrophosphate synthase

Short name=FPP synthase
Short name=FPS
EC=2.5.1.10
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Geranyltranstransferase
Gene names
Name:ERG20
Synonyms:BOT3, FDS1, FPP1
Ordered Locus Names:YJL167W
ORF Names:J0525
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate.

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Pathway

Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.

Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Farnesyl pyrophosphate synthase
PRO_0000123952

Sites

Metal binding1001Magnesium 1 By similarity
Metal binding1001Magnesium 2 By similarity
Metal binding1041Magnesium 1 By similarity
Metal binding1041Magnesium 2 By similarity
Metal binding2401Magnesium 3 By similarity
Binding site521Isopentenyl diphosphate By similarity
Binding site551Isopentenyl diphosphate By similarity
Binding site931Isopentenyl diphosphate By similarity
Binding site1091Dimethylallyl diphosphate By similarity
Binding site1101Isopentenyl diphosphate By similarity
Binding site1971Dimethylallyl diphosphate By similarity
Binding site1981Dimethylallyl diphosphate By similarity
Binding site2371Dimethylallyl diphosphate By similarity
Binding site2541Dimethylallyl diphosphate By similarity
Binding site2631Dimethylallyl diphosphate By similarity

Experimental info

Mutagenesis1971K → E in ERG20-2; 14-fold decrease in FPPS activity.

Sequences

Sequence LengthMass (Da)Tools
P08524 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: 79A357BB7BFCEDDA

FASTA35240,483
        10         20         30         40         50         60 
MASEKEIRRE RFLNVFPKLV EELNASLLAY GMPKEACDWY AHSLNYNTPG GKLNRGLSVV 

        70         80         90        100        110        120 
DTYAILSNKT VEQLGQEEYE KVAILGWCIE LLQAYFLVAD DMMDKSITRR GQPCWYKVPE 

       130        140        150        160        170        180 
VGEIAINDAF MLEAAIYKLL KSHFRNEKYY IDITELFHEV TFQTELGQLM DLITAPEDKV 

       190        200        210        220        230        240 
DLSKFSLKKH SFIVTFKTAY YSFYLPVALA MYVAGITDEK DLKQARDVLI PLGEYFQIQD 

       250        260        270        280        290        300 
DYLDCFGTPE QIGKIGTDIQ DNKCSWVINK ALELASAEQR KTLDENYGKK DSVAEAKCKK 

       310        320        330        340        350 
IFNDLKIEQL YHEYEESIAK DLKAKISQVD ESRGFKADVL TAFLNKVYKR SK 

« Hide

References

« Hide 'large scale' references
[1]"Farnesyl diphosphate synthetase. Molecular cloning, sequence, and expression of an essential gene from Saccharomyces cerevisiae."
Anderson M.S., Yarger J.G., Burck C.L., Poulter C.D.
J. Biol. Chem. 264:19176-19184(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
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. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Nucleotide sequence of the gene encoding the 11-kDa subunit of the ubiquinol-cytochrome-c oxidoreductase in Saccharomyces cerevisiae."
Maarse A.C., Grivell L.A.
Eur. J. Biochem. 165:419-425(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 131-352.
[5]"Characterization of a lysine-to-glutamic acid mutation in a conservative sequence of farnesyl diphosphate synthase from Saccharomyces cerevisiae."
Blanchard L., Karst F.
Gene 125:185-189(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTANT GLU-197.
Strain: LB25.
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05091 Genomic DNA. Translation: AAA34606.1.
Z49442 Genomic DNA. Translation: CAA89462.1.
X05550 Genomic DNA. Translation: CAA29064.1.
BK006943 Genomic DNA. Translation: DAA08636.1.
PIRA34441.
RefSeqNP_012368.1. NM_001181600.1.

3D structure databases

ProteinModelPortalP08524.
SMRP08524. Positions 11-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33592. 53 interactions.
DIPDIP-1163N.
IntActP08524. 3 interactions.
MINTMINT-555012.
STRING4932.YJL167W.

Proteomic databases

PaxDbP08524.
PeptideAtlasP08524.
PRIDEP08524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL167W; YJL167W; YJL167W.
GeneID853272.
KEGGsce:YJL167W.

Organism-specific databases

CYGDYJL167w.
SGDS000003703. ERG20.

Phylogenomic databases

eggNOGCOG0142.
GeneTreeENSGT00530000064127.
HOGENOMHOG000160912.
KOK00787.
OMAVALAMRM.
OrthoDBEOG79GTJ1.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-655.
YEAST:MONOMER-655.
YEAST:YJL167W-MONOMER.
UniPathwayUPA00259; UER00368.
UPA00260; UER00369.

Gene expression databases

GenevestigatorP08524.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio973547.
PROP08524.

Entry information

Entry nameFPPS_YEAST
AccessionPrimary (citable) accession number: P08524
Secondary accession number(s): D6VW20, P15495
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways