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P08836

- FPPS_CHICK

UniProt

P08836 - FPPS_CHICK

Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      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.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 711Isopentenyl diphosphateBy similarity
    Binding sitei74 – 741Isopentenyl diphosphateBy similarity
    Binding sitei110 – 1101Isopentenyl diphosphateBy similarity
    Sitei112 – 1121Important for determining product chain length
    Sitei113 – 1131Important for determining product chain length
    Metal bindingi117 – 1171Magnesium 1
    Metal bindingi117 – 1171Magnesium 2
    Metal bindingi121 – 1211Magnesium 1
    Metal bindingi121 – 1211Magnesium 2
    Binding sitei126 – 1261Dimethylallyl diphosphate
    Binding sitei127 – 1271Isopentenyl diphosphateBy similarity
    Binding sitei214 – 2141Dimethylallyl diphosphate
    Binding sitei215 – 2151Dimethylallyl diphosphateBy similarity
    Binding sitei254 – 2541Dimethylallyl diphosphateBy similarity
    Metal bindingi257 – 2571Magnesium 3By similarity
    Binding sitei271 – 2711Dimethylallyl diphosphateBy similarity
    Binding sitei280 – 2801Dimethylallyl diphosphate

    GO - Molecular functioni

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

    GO - Biological processi

    1. cholesterol biosynthetic process Source: UniProtKB-KW
    2. farnesyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
    3. geranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Cholesterol biosynthesis, Cholesterol metabolism, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    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:FDPS
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi112 – 1121F → A: Alters selectivity towards product chain length, so that geranylgeranyl diphosphate is produced. 1 Publication
    Mutagenesisi113 – 1131F → S: Alters selectivity towards product chain length, so that geranylfarnesyl diphosphate is produced. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 367367Farnesyl pyrophosphate synthasePRO_0000123947Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    367
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 3313
    Helixi35 – 439
    Turni44 – 463
    Turni50 – 523
    Helixi53 – 6614
    Beta strandi67 – 704
    Helixi73 – 8513
    Helixi88 – 903
    Helixi93 – 12129
    Helixi132 – 1343
    Turni136 – 1405
    Helixi141 – 16121
    Beta strandi162 – 1643
    Helixi167 – 19125
    Beta strandi194 – 1963
    Beta strandi199 – 2013
    Helixi204 – 21411
    Helixi216 – 2194
    Helixi221 – 23111
    Helixi236 – 26328
    Turni266 – 2694
    Beta strandi276 – 2783
    Helixi283 – 2919
    Helixi294 – 30310
    Beta strandi304 – 3074
    Helixi309 – 32214
    Helixi324 – 34623
    Beta strandi348 – 3503
    Helixi353 – 36210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FPSX-ray2.60A20-367[»]
    1UBVX-ray2.50A1-367[»]
    1UBWX-ray2.50A1-367[»]
    1UBXX-ray2.50A1-367[»]
    1UBYX-ray2.40A1-367[»]
    ProteinModelPortaliP08836.
    SMRiP08836. Positions 20-367.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08836.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FPP/GGPP synthase family.Curated

    Phylogenomic databases

    HOVERGENiHBG005741.
    PhylomeDBiP08836.

    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.

    P08836-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHKFTGVNAK FQQPALRNLS PVVVEREREE FVGFFPQIVR DLTEDGIGHP    50
    EVGDAVARLK EVLQYNAPGG KCNRGLTVVA AYRELSGPGQ KDAESLRCAL 100
    AVGWCIELFQ AFFLVADDIM DQSLTRRGQL CWYKKEGVGL DAINDSFLLE 150
    SSVYRVLKKY CRQRPYYVHL LELFLQTAYQ TELGQMLDLI TAPVSKVDLS 200
    HFSEERYKAI VKYKTAFYSF YLPVAAAMYM VGIDSKEEHE NAKAILLEMG 250
    EYFQIQDDYL DCFGDPALTG KVGTDIQDNK CSWLVVQCLQ RVTPEQRQLL 300
    EDNYGRKEPE KVAKVKELYE AVGMRAAFQQ YEESSYRRLQ ELIEKHSNRL 350
    PKEIFLGLAQ KIYKRQK 367
    Length:367
    Mass (Da):42,153
    Last modified:December 15, 1998 - v2
    Checksum:iBB23D29D62CD842B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911T → G AA sequence (PubMed:7272273)Curated
    Sequence conflicti201 – 2033HFS → TFQ AA sequence (PubMed:7272273)Curated
    Sequence conflicti210 – 2123IVK → FVP AA sequence (PubMed:7272273)Curated
    Sequence conflicti215 – 2162TA → AM AA sequence (PubMed:7272273)Curated

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FPS X-ray 2.60 A 20-367 [» ]
    1UBV X-ray 2.50 A 1-367 [» ]
    1UBW X-ray 2.50 A 1-367 [» ]
    1UBX X-ray 2.50 A 1-367 [» ]
    1UBY X-ray 2.40 A 1-367 [» ]
    ProteinModelPortali P08836.
    SMRi P08836. Positions 20-367.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005741.
    PhylomeDBi P08836.

    Enzyme and pathway databases

    UniPathwayi UPA00259 ; UER00368 .
    UPA00260 ; UER00369 .

    Miscellaneous databases

    EvolutionaryTracei P08836.

    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. "Isolation and characterization of a photoaffinity-labeled peptide from the catalytic site of prenyltransferase."
      Brems D.N., Bruenger E., Rillings H.C.
      Biochemistry 20:3711-3718(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 187-216.
      Tissue: Liver.
    2. "Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution."
      Tarshis L.C., Yan M., Poulter C.D., Sacchettini J.C.
      Biochemistry 33:10871-10877(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-367, SUBUNIT, COFACTOR.
      Tissue: Liver.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-367 IN COMPLEXES WITH MAGNESIUM IONS; DIMETHYLALLYL DIPHOSPHATE; GERANYL DIPHOSPHATE AND FARNESYL DIPHOSPHATE, MUTAGENESIS OF PHE-112 AND PHE-113, SUBUNIT.
      Tissue: Liver.

    Entry informationi

    Entry nameiFPPS_CHICK
    AccessioniPrimary (citable) accession number: P08836
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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

    External Data

    Dasty 3