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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361Isopentenyl diphosphate1 Publication
    Binding sitei39 – 391Isopentenyl diphosphate1 Publication
    Binding sitei68 – 681Isopentenyl diphosphate1 Publication
    Metal bindingi75 – 751Magnesium 12 Publications
    Metal bindingi75 – 751Magnesium 22 Publications
    Metal bindingi79 – 791Magnesium 12 Publications
    Metal bindingi79 – 791Magnesium 22 Publications
    Binding sitei84 – 841Dimethylallyl diphosphate1 Publication
    Binding sitei85 – 851Isopentenyl diphosphate1 Publication
    Sitei107 – 1071Important for determining product chain length
    Binding sitei169 – 1691Dimethylallyl diphosphate1 Publication
    Binding sitei170 – 1701Dimethylallyl diphosphate1 Publication
    Binding sitei206 – 2061Dimethylallyl diphosphate1 Publication
    Metal bindingi209 – 2091Magnesium 32 Publications
    Binding sitei213 – 2131Dimethylallyl diphosphate1 Publication
    Binding sitei223 – 2231Dimethylallyl diphosphateBy similarity
    Binding sitei233 – 2331Dimethylallyl diphosphate1 Publication

    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:MONOMER-13701.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71E → G: No effect. Monomer; when associated with G-8. 1 Publication
    Mutagenesisi8 – 81L → G: Monomer and homodimer. Monomer; when associated with G-7. 1 Publication
    Mutagenesisi9 – 91I → G: Mostly monomer. Exclusively monomer; when associated with G-8. Reduces enzyme activity 1000-fold. 1 Publication
    Mutagenesisi107 – 1071Y → A: Reduced affinity for isopentenyl diphosphate (IPP).
    Mutagenesisi108 – 1081F → A: Reduced affinity for isopentenyl diphosphate (IPP).
    Mutagenesisi139 – 1391H → A: Reduced affinity for isopentenyl diphosphate (IPP).

    Chemistry

    ChEMBLiCHEMBL1075251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 335335Geranylgeranyl pyrophosphate synthasePRO_0000228139Add
    BLAST

    Proteomic databases

    MaxQBiQ12051.

    Interactioni

    Protein-protein interaction databases

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

    Chemistry

    BindingDBiQ12051.

    Structurei

    Secondary structure

    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 99Combined sources
    Helixi17 – 3115Combined sources
    Beta strandi32 – 343Combined sources
    Helixi38 – 5013Combined sources
    Helixi54 – 7825Combined sources
    Beta strandi82 – 843Combined sources
    Helixi90 – 934Combined sources
    Helixi96 – 11318Combined sources
    Helixi114 – 1174Combined sources
    Helixi121 – 15030Combined sources
    Turni151 – 1533Combined sources
    Helixi159 – 16911Combined sources
    Helixi171 – 18414Combined sources
    Helixi195 – 21521Combined sources
    Turni221 – 2233Combined sources
    Helixi227 – 2304Combined sources
    Helixi236 – 24712Combined sources
    Helixi251 – 26313Combined sources
    Helixi268 – 28013Combined sources
    Helixi284 – 30017Combined sources
    Helixi325 – 3306Combined sources
    Turni331 – 3333Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-335.
    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.
    IPR017446. Polyprenyl_synth-rel.
    [Graphical view]
    PANTHERiPTHR12001. PTHR12001. 1 hit.
    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
    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. Positions 1-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry

    BindingDBiQ12051.
    ChEMBLiCHEMBL1075251.

    Proteomic databases

    MaxQBiQ12051.

    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:MONOMER-13701.
    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.
    IPR017446. Polyprenyl_synth-rel.
    [Graphical view]
    PANTHERiPTHR12001. PTHR12001. 1 hit.
    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: September 7, 2016
    This is version 130 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.