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Protein

Farnesyl pyrophosphate synthase

Gene

FDPS

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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

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

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. Farnesyl pyrophosphate synthase (FDPS)
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. Farnesyl pyrophosphate synthase (FDPS)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei71Isopentenyl diphosphateBy similarity1
Binding sitei74Isopentenyl diphosphateBy similarity1
Binding sitei110Isopentenyl diphosphateBy similarity1
Sitei112Important for determining product chain length1
Sitei113Important for determining product chain length1
Metal bindingi117Magnesium 11
Metal bindingi117Magnesium 21
Metal bindingi121Magnesium 11
Metal bindingi121Magnesium 21
Binding sitei126Dimethylallyl diphosphate1
Binding sitei127Isopentenyl diphosphateBy similarity1
Binding sitei214Dimethylallyl diphosphate1
Binding sitei215Dimethylallyl diphosphateBy similarity1
Binding sitei254Dimethylallyl diphosphateBy similarity1
Metal bindingi257Magnesium 3By similarity1
Binding sitei271Dimethylallyl diphosphateBy similarity1
Binding sitei280Dimethylallyl diphosphate1

GO - Molecular functioni

GO - Biological processi

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112F → A: Alters selectivity towards product chain length, so that geranylgeranyl diphosphate is produced. 1 Publication1
Mutagenesisi113F → S: Alters selectivity towards product chain length, so that geranylfarnesyl diphosphate is produced. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001239471 – 367Farnesyl pyrophosphate synthaseAdd BLAST367

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1367
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 33Combined sources13
Helixi35 – 43Combined sources9
Turni44 – 46Combined sources3
Turni50 – 52Combined sources3
Helixi53 – 66Combined sources14
Beta strandi67 – 70Combined sources4
Helixi73 – 85Combined sources13
Helixi88 – 90Combined sources3
Helixi93 – 121Combined sources29
Helixi132 – 134Combined sources3
Turni136 – 140Combined sources5
Helixi141 – 161Combined sources21
Beta strandi162 – 164Combined sources3
Helixi167 – 191Combined sources25
Beta strandi194 – 196Combined sources3
Beta strandi199 – 201Combined sources3
Helixi204 – 214Combined sources11
Helixi216 – 219Combined sources4
Helixi221 – 231Combined sources11
Helixi236 – 263Combined sources28
Turni266 – 269Combined sources4
Beta strandi276 – 278Combined sources3
Helixi283 – 291Combined sources9
Helixi294 – 303Combined sources10
Beta strandi304 – 307Combined sources4
Helixi309 – 322Combined sources14
Helixi324 – 346Combined sources23
Beta strandi348 – 350Combined sources3
Helixi353 – 362Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti191T → G AA sequence (PubMed:7272273).Curated1
Sequence conflicti201 – 203HFS → TFQ AA sequence (PubMed:7272273).Curated3
Sequence conflicti210 – 212IVK → FVP AA sequence (PubMed:7272273).Curated3
Sequence conflicti215 – 216TA → AM AA sequence (PubMed:7272273).Curated2

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005741.
InParanoidiP08836.
PhylomeDBiP08836.

Enzyme and pathway databases

UniPathwayiUPA00259; UER00368.
UPA00260; UER00369.

Miscellaneous databases

EvolutionaryTraceiP08836.

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 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: November 30, 2016
This is version 106 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

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.