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P08524

- FPPS_YEAST

UniProt

P08524 - FPPS_YEAST

Protein

Farnesyl pyrophosphate synthase

Gene

ERG20

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521Isopentenyl diphosphateBy similarity
    Binding sitei55 – 551Isopentenyl diphosphateBy similarity
    Binding sitei93 – 931Isopentenyl diphosphateBy similarity
    Metal bindingi100 – 1001Magnesium 1By similarity
    Metal bindingi100 – 1001Magnesium 2By similarity
    Metal bindingi104 – 1041Magnesium 1By similarity
    Metal bindingi104 – 1041Magnesium 2By similarity
    Binding sitei109 – 1091Dimethylallyl diphosphateBy similarity
    Binding sitei110 – 1101Isopentenyl diphosphateBy similarity
    Binding sitei197 – 1971Dimethylallyl diphosphateBy similarity
    Binding sitei198 – 1981Dimethylallyl diphosphateBy similarity
    Binding sitei237 – 2371Dimethylallyl diphosphateBy similarity
    Metal bindingi240 – 2401Magnesium 3By similarity
    Binding sitei254 – 2541Dimethylallyl diphosphateBy similarity
    Binding sitei263 – 2631Dimethylallyl diphosphateBy similarity

    GO - Molecular functioni

    1. dimethylallyltranstransferase activity Source: SGD
    2. geranyltranstransferase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. ergosterol biosynthetic process Source: SGD
    2. farnesyl diphosphate biosynthetic process Source: SGD
    3. geranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
    4. isoprenoid biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-655.
    YEAST:MONOMER-655.
    ReactomeiREACT_188982. Activation of gene expression by SREBF (SREBP).
    UniPathwayiUPA00259; UER00368.
    UPA00260; UER00369.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Farnesyl pyrophosphate synthase (EC:2.5.1.10)
    Short name:
    FPP synthase
    Short name:
    FPS
    Alternative name(s):
    (2E,6E)-farnesyl diphosphate synthase
    Dimethylallyltranstransferase (EC:2.5.1.1)
    Farnesyl diphosphate synthase
    Geranyltranstransferase
    Gene namesi
    Name:ERG20
    Synonyms:BOT3, FDS1, FPP1
    Ordered Locus Names:YJL167W
    ORF Names:J0525
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL167w.
    SGDiS000003703. ERG20.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. endoplasmic reticulum Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi197 – 1971K → E in ERG20-2; 14-fold decrease in FPPS activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 352352Farnesyl pyrophosphate synthasePRO_0000123952Add
    BLAST

    Proteomic databases

    MaxQBiP08524.
    PaxDbiP08524.
    PeptideAtlasiP08524.
    PRIDEiP08524.

    Expressioni

    Gene expression databases

    GenevestigatoriP08524.

    Interactioni

    Protein-protein interaction databases

    BioGridi33592. 53 interactions.
    DIPiDIP-1163N.
    IntActiP08524. 3 interactions.
    MINTiMINT-555012.
    STRINGi4932.YJL167W.

    Structurei

    3D structure databases

    ProteinModelPortaliP08524.
    SMRiP08524. Positions 11-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FPP/GGPP synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0142.
    GeneTreeiENSGT00530000064127.
    HOGENOMiHOG000160912.
    KOiK00787.
    OMAiLEACYGR.
    OrthoDBiEOG79GTJ1.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR000092. Polyprenyl_synt.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PfamiPF00348. polyprenyl_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF48576. SSF48576. 1 hit.
    PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
    PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08524-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASEKEIRRE RFLNVFPKLV EELNASLLAY GMPKEACDWY AHSLNYNTPG    50
    GKLNRGLSVV DTYAILSNKT VEQLGQEEYE KVAILGWCIE LLQAYFLVAD 100
    DMMDKSITRR GQPCWYKVPE VGEIAINDAF MLEAAIYKLL KSHFRNEKYY 150
    IDITELFHEV TFQTELGQLM DLITAPEDKV DLSKFSLKKH SFIVTFKTAY 200
    YSFYLPVALA MYVAGITDEK DLKQARDVLI PLGEYFQIQD DYLDCFGTPE 250
    QIGKIGTDIQ DNKCSWVINK ALELASAEQR KTLDENYGKK DSVAEAKCKK 300
    IFNDLKIEQL YHEYEESIAK DLKAKISQVD ESRGFKADVL TAFLNKVYKR 350
    SK 352
    Length:352
    Mass (Da):40,483
    Last modified:November 1, 1991 - v2
    Checksum:i79A357BB7BFCEDDA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05091 Genomic DNA. Translation: AAA34606.1.
    Z49442 Genomic DNA. Translation: CAA89462.1.
    X05550 Genomic DNA. Translation: CAA29064.1.
    BK006943 Genomic DNA. Translation: DAA08636.1.
    PIRiA34441.
    RefSeqiNP_012368.1. NM_001181600.1.

    Genome annotation databases

    EnsemblFungiiYJL167W; YJL167W; YJL167W.
    GeneIDi853272.
    KEGGisce:YJL167W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05091 Genomic DNA. Translation: AAA34606.1 .
    Z49442 Genomic DNA. Translation: CAA89462.1 .
    X05550 Genomic DNA. Translation: CAA29064.1 .
    BK006943 Genomic DNA. Translation: DAA08636.1 .
    PIRi A34441.
    RefSeqi NP_012368.1. NM_001181600.1.

    3D structure databases

    ProteinModelPortali P08524.
    SMRi P08524. Positions 11-352.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33592. 53 interactions.
    DIPi DIP-1163N.
    IntActi P08524. 3 interactions.
    MINTi MINT-555012.
    STRINGi 4932.YJL167W.

    Proteomic databases

    MaxQBi P08524.
    PaxDbi P08524.
    PeptideAtlasi P08524.
    PRIDEi P08524.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL167W ; YJL167W ; YJL167W .
    GeneIDi 853272.
    KEGGi sce:YJL167W.

    Organism-specific databases

    CYGDi YJL167w.
    SGDi S000003703. ERG20.

    Phylogenomic databases

    eggNOGi COG0142.
    GeneTreei ENSGT00530000064127.
    HOGENOMi HOG000160912.
    KOi K00787.
    OMAi LEACYGR.
    OrthoDBi EOG79GTJ1.

    Enzyme and pathway databases

    UniPathwayi UPA00259 ; UER00368 .
    UPA00260 ; UER00369 .
    BioCyci MetaCyc:MONOMER-655.
    YEAST:MONOMER-655.
    Reactomei REACT_188982. Activation of gene expression by SREBF (SREBP).

    Miscellaneous databases

    NextBioi 973547.
    PROi P08524.

    Gene expression databases

    Genevestigatori P08524.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR000092. Polyprenyl_synt.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    Pfami PF00348. polyprenyl_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    PROSITEi PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
    PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiFPPS_YEAST
    AccessioniPrimary (citable) accession number: P08524
    Secondary accession number(s): D6VW20, P15495
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3