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P08836

- FPPS_CHICK

UniProt

P08836 - FPPS_CHICK

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Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
InParanoidiP08836.
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

        10         20         30         40         50
MHKFTGVNAK FQQPALRNLS PVVVEREREE FVGFFPQIVR DLTEDGIGHP
60 70 80 90 100
EVGDAVARLK EVLQYNAPGG KCNRGLTVVA AYRELSGPGQ KDAESLRCAL
110 120 130 140 150
AVGWCIELFQ AFFLVADDIM DQSLTRRGQL CWYKKEGVGL DAINDSFLLE
160 170 180 190 200
SSVYRVLKKY CRQRPYYVHL LELFLQTAYQ TELGQMLDLI TAPVSKVDLS
210 220 230 240 250
HFSEERYKAI VKYKTAFYSF YLPVAAAMYM VGIDSKEEHE NAKAILLEMG
260 270 280 290 300
EYFQIQDDYL DCFGDPALTG KVGTDIQDNK CSWLVVQCLQ RVTPEQRQLL
310 320 330 340 350
EDNYGRKEPE KVAKVKELYE AVGMRAAFQQ YEESSYRRLQ ELIEKHSNRL
360
PKEIFLGLAQ KIYKRQK
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.
InParanoidi P08836.
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 29, 2014
This is version 96 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