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Protein

Geranylgeranyl pyrophosphate synthase

Gene

BTS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of YPT1 and SEC4. May be involved in vesicle trafficking and protein sorting.2 Publications

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 3 Mg2+ ions per subunit.1 Publication

Kineticsi

  1. KM=3.2 µM for farnesyl diphosphate
  2. KM=0.8 µM for isopentenyl diphosphate

    Pathwayi: farnesyl diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Geranylgeranyl pyrophosphate synthase (BTS1), Farnesyl pyrophosphate synthase (ERG20)
    This subpathway is part of the pathway farnesyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate, the pathway farnesyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

    Pathwayi: geranyl diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Geranylgeranyl pyrophosphate synthase (BTS1), Farnesyl pyrophosphate synthase (ERG20)
    This subpathway is part of the pathway geranyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate, the pathway geranyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

    Pathwayi: geranylgeranyl diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Geranylgeranyl pyrophosphate synthase (BTS1)
    This subpathway is part of the pathway geranylgeranyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate, the pathway geranylgeranyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei36Isopentenyl diphosphate1 Publication1
    Binding sitei39Isopentenyl diphosphate1 Publication1
    Binding sitei68Isopentenyl diphosphate1 Publication1
    Metal bindingi75Magnesium 12 Publications1
    Metal bindingi75Magnesium 22 Publications1
    Metal bindingi79Magnesium 12 Publications1
    Metal bindingi79Magnesium 22 Publications1
    Binding sitei84Dimethylallyl diphosphate1 Publication1
    Binding sitei85Isopentenyl diphosphate1 Publication1
    Sitei107Important for determining product chain length1
    Binding sitei169Dimethylallyl diphosphate1 Publication1
    Binding sitei170Dimethylallyl diphosphate1 Publication1
    Binding sitei206Dimethylallyl diphosphate1 Publication1
    Metal bindingi209Magnesium 32 Publications1
    Binding sitei213Dimethylallyl diphosphate1 Publication1
    Binding sitei223Dimethylallyl diphosphateBy similarity1
    Binding sitei233Dimethylallyl diphosphate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carotenoid biosynthesis, Isoprene biosynthesis, Protein transport, Transport

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:YPL069C-MONOMER.
    YEAST:YPL069C-MONOMER.
    BRENDAi2.5.1.29. 984.
    ReactomeiR-SCE-191273. Cholesterol biosynthesis.
    SABIO-RKQ12051.
    UniPathwayiUPA00259; UER00368.
    UPA00260; UER00369.
    UPA00389; UER00564.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Geranylgeranyl pyrophosphate synthase (EC:2.5.1.-)
    Short name:
    GGPP synthase
    Short name:
    GGPPSase
    Alternative name(s):
    (2E,6E)-farnesyl diphosphate synthase
    BET2 suppressor protein 1
    Dimethylallyltranstransferase (EC:2.5.1.1)
    Farnesyl diphosphate synthase
    Farnesyltranstransferase (EC:2.5.1.29)
    Geranylgeranyl diphosphate synthase
    Geranyltranstransferase (EC:2.5.1.10)
    Gene namesi
    Name:BTS1
    Ordered Locus Names:YPL069C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XVI

    Organism-specific databases

    EuPathDBiFungiDB:YPL069C.
    SGDiS000005990. BTS1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi7E → G: No effect. Monomer; when associated with G-8. 1 Publication1
    Mutagenesisi8L → G: Monomer and homodimer. Monomer; when associated with G-7. 1 Publication1
    Mutagenesisi9I → G: Mostly monomer. Exclusively monomer; when associated with G-8. Reduces enzyme activity 1000-fold. 1 Publication1
    Mutagenesisi107Y → A: Reduced affinity for isopentenyl diphosphate (IPP). 1
    Mutagenesisi108F → A: Reduced affinity for isopentenyl diphosphate (IPP). 1
    Mutagenesisi139H → A: Reduced affinity for isopentenyl diphosphate (IPP). 1

    Chemistry databases

    ChEMBLiCHEMBL1075251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002281391 – 335Geranylgeranyl pyrophosphate synthaseAdd BLAST335

    Proteomic databases

    MaxQBiQ12051.
    PRIDEiQ12051.

    Interactioni

    Protein-protein interaction databases

    BioGridi36110. 317 interactors.
    DIPiDIP-8889N.
    IntActiQ12051. 5 interactors.
    MINTiMINT-4504645.

    Chemistry databases

    BindingDBiQ12051.

    Structurei

    Secondary structure

    1335
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi1 – 9Combined sources9
    Helixi17 – 31Combined sources15
    Beta strandi32 – 34Combined sources3
    Helixi38 – 50Combined sources13
    Helixi54 – 78Combined sources25
    Beta strandi82 – 84Combined sources3
    Helixi90 – 93Combined sources4
    Helixi96 – 113Combined sources18
    Helixi114 – 117Combined sources4
    Helixi121 – 150Combined sources30
    Turni151 – 153Combined sources3
    Helixi159 – 169Combined sources11
    Helixi171 – 184Combined sources14
    Helixi195 – 215Combined sources21
    Turni221 – 223Combined sources3
    Helixi227 – 230Combined sources4
    Helixi236 – 247Combined sources12
    Helixi251 – 263Combined sources13
    Helixi268 – 280Combined sources13
    Helixi284 – 300Combined sources17
    Helixi325 – 330Combined sources6
    Turni331 – 333Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2DH4X-ray1.98A/B1-335[»]
    2E8TX-ray2.13A/B1-335[»]
    2E8UX-ray2.08A/B1-335[»]
    2E8VX-ray1.80A/B1-335[»]
    2E8WX-ray2.35A/B1-335[»]
    2E8XX-ray2.04A/B1-335[»]
    2E90X-ray2.55A/B1-335[»]
    2E91X-ray2.14A/B1-335[»]
    2E92X-ray2.31A/B1-335[»]
    2E93X-ray2.12A/B1-335[»]
    2E94X-ray2.18A/B1-335[»]
    2E95X-ray2.20A/B1-335[»]
    2Z4VX-ray1.86A/B1-335[»]
    2Z4WX-ray2.45A/B1-335[»]
    2Z4XX-ray1.90A/B1-335[»]
    2Z4YX-ray2.10A/B1-335[»]
    2Z4ZX-ray2.09A/B1-335[»]
    2Z50X-ray2.01A/B1-335[»]
    2Z52X-ray2.13A/B1-335[»]
    2Z78X-ray2.10A/B1-335[»]
    2Z7HX-ray2.08A/B1-335[»]
    2Z7IX-ray2.10A/B1-335[»]
    2ZEUX-ray2.00A/B1-335[»]
    2ZEVX-ray2.23A/B1-335[»]
    ProteinModelPortaliQ12051.
    SMRiQ12051.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12051.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FPP/GGPP synthase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000010417.
    HOGENOMiHOG000169461.
    InParanoidiQ12051.
    KOiK00804.
    OMAiNKGYAED.
    OrthoDBiEOG092C3Q3X.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR000092. Polyprenyl_synt.
    IPR033749. Polyprenyl_synt_CS.
    [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.

    Q12051-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEAKIDELIN NDPVWSSQNE SLISKPYNHI LLKPGKNFRL NLIVQINRVM
    60 70 80 90 100
    NLPKDQLAIV SQIVELLHNS SLLIDDIEDN APLRRGQTTS HLIFGVPSTI
    110 120 130 140 150
    NTANYMYFRA MQLVSQLTTK EPLYHNLITI FNEELINLHR GQGLDIYWRD
    160 170 180 190 200
    FLPEIIPTQE MYLNMVMNKT GGLFRLTLRL MEALSPSSHH GHSLVPFINL
    210 220 230 240 250
    LGIIYQIRDD YLNLKDFQMS SEKGFAEDIT EGKLSFPIVH ALNFTKTKGQ
    260 270 280 290 300
    TEQHNEILRI LLLRTSDKDI KLKLIQILEF DTNSLAYTKN FINQLVNMIK
    310 320 330
    NDNENKYLPD LASHSDTATN LHDELLYIID HLSEL
    Length:335
    Mass (Da):38,651
    Last modified:November 1, 1996 - v1
    Checksum:i4C7D6527FF29F157
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U39205 Genomic DNA. Translation: AAB68296.1.
    U31632 Genomic DNA. Translation: AAA83262.1.
    AY692852 Genomic DNA. Translation: AAT92871.1.
    BK006949 Genomic DNA. Translation: DAA11362.1.
    PIRiS60921.
    RefSeqiNP_015256.1. NM_001183883.1.

    Genome annotation databases

    EnsemblFungiiYPL069C; YPL069C; YPL069C.
    GeneIDi856036.
    KEGGisce:YPL069C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U39205 Genomic DNA. Translation: AAB68296.1.
    U31632 Genomic DNA. Translation: AAA83262.1.
    AY692852 Genomic DNA. Translation: AAT92871.1.
    BK006949 Genomic DNA. Translation: DAA11362.1.
    PIRiS60921.
    RefSeqiNP_015256.1. NM_001183883.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2DH4X-ray1.98A/B1-335[»]
    2E8TX-ray2.13A/B1-335[»]
    2E8UX-ray2.08A/B1-335[»]
    2E8VX-ray1.80A/B1-335[»]
    2E8WX-ray2.35A/B1-335[»]
    2E8XX-ray2.04A/B1-335[»]
    2E90X-ray2.55A/B1-335[»]
    2E91X-ray2.14A/B1-335[»]
    2E92X-ray2.31A/B1-335[»]
    2E93X-ray2.12A/B1-335[»]
    2E94X-ray2.18A/B1-335[»]
    2E95X-ray2.20A/B1-335[»]
    2Z4VX-ray1.86A/B1-335[»]
    2Z4WX-ray2.45A/B1-335[»]
    2Z4XX-ray1.90A/B1-335[»]
    2Z4YX-ray2.10A/B1-335[»]
    2Z4ZX-ray2.09A/B1-335[»]
    2Z50X-ray2.01A/B1-335[»]
    2Z52X-ray2.13A/B1-335[»]
    2Z78X-ray2.10A/B1-335[»]
    2Z7HX-ray2.08A/B1-335[»]
    2Z7IX-ray2.10A/B1-335[»]
    2ZEUX-ray2.00A/B1-335[»]
    2ZEVX-ray2.23A/B1-335[»]
    ProteinModelPortaliQ12051.
    SMRiQ12051.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36110. 317 interactors.
    DIPiDIP-8889N.
    IntActiQ12051. 5 interactors.
    MINTiMINT-4504645.

    Chemistry databases

    BindingDBiQ12051.
    ChEMBLiCHEMBL1075251.

    Proteomic databases

    MaxQBiQ12051.
    PRIDEiQ12051.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYPL069C; YPL069C; YPL069C.
    GeneIDi856036.
    KEGGisce:YPL069C.

    Organism-specific databases

    EuPathDBiFungiDB:YPL069C.
    SGDiS000005990. BTS1.

    Phylogenomic databases

    GeneTreeiENSGT00390000010417.
    HOGENOMiHOG000169461.
    InParanoidiQ12051.
    KOiK00804.
    OMAiNKGYAED.
    OrthoDBiEOG092C3Q3X.

    Enzyme and pathway databases

    UniPathwayiUPA00259; UER00368.
    UPA00260; UER00369.
    UPA00389; UER00564.
    BioCyciMetaCyc:YPL069C-MONOMER.
    YEAST:YPL069C-MONOMER.
    BRENDAi2.5.1.29. 984.
    ReactomeiR-SCE-191273. Cholesterol biosynthesis.
    SABIO-RKQ12051.

    Miscellaneous databases

    EvolutionaryTraceiQ12051.
    PROiQ12051.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR000092. Polyprenyl_synt.
    IPR033749. Polyprenyl_synt_CS.
    [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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGGPPS_YEAST
    AccessioniPrimary (citable) accession number: Q12051
    Secondary accession number(s): D6W3U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: November 1, 1996
    Last modified: November 30, 2016
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2840 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.