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Protein

Farnesyl pyrophosphate synthase

Gene

Fdps

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Enzyme regulationi

Inactivated by interferon-induced RSAD2. This inactivation may result of disruption of lipid rafts at the plasma membrane, and thus have an antiviral effect since many enveloped viruses need lipid rafts to bud efficiently out of the cell (By similarity).By similarity

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), Geranylgeranyl pyrophosphate synthase (Ggps1)
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), Geranylgeranyl pyrophosphate synthase (Ggps1)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei57 – 571Isopentenyl diphosphateBy similarity
Binding sitei60 – 601Isopentenyl diphosphateBy similarity
Binding sitei96 – 961Isopentenyl diphosphateBy similarity
Sitei98 – 981Important for determining product chain lengthBy similarity
Sitei99 – 991Important for determining product chain lengthBy similarity
Metal bindingi103 – 1031Magnesium 1By similarity
Metal bindingi103 – 1031Magnesium 2By similarity
Metal bindingi107 – 1071Magnesium 1By similarity
Metal bindingi107 – 1071Magnesium 2By similarity
Binding sitei112 – 1121Dimethylallyl diphosphateBy similarity
Binding sitei113 – 1131Isopentenyl diphosphateBy similarity
Binding sitei200 – 2001Dimethylallyl diphosphateBy similarity
Binding sitei201 – 2011Dimethylallyl diphosphateBy similarity
Binding sitei240 – 2401Dimethylallyl diphosphateBy similarity
Metal bindingi243 – 2431Magnesium 3By similarity
Binding sitei257 – 2571Dimethylallyl diphosphateBy similarity
Binding sitei266 – 2661Dimethylallyl diphosphateBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to fatty acid Source: RGD
  • cholesterol biosynthetic process Source: RGD
  • farnesyl diphosphate biosynthetic process Source: RGD
  • geranyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
  • isoprenoid biosynthetic process Source: RGD
  • male gonad development Source: RGD
  • positive regulation of cell growth involved in cardiac muscle cell development Source: RGD
  • positive regulation of cholesterol biosynthetic process Source: RGD
  • response to cholesterol Source: RGD
  • response to drug Source: RGD
  • response to peptide hormone Source: RGD
  • response to testosterone Source: RGD
  • spermatogenesis Source: RGD
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

SABIO-RKP05369.
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
Cholesterol-regulated 39 kDa protein
Short name:
CR 39
Dimethylallyltranstransferase (EC:2.5.1.1)
Farnesyl diphosphate synthase
Geranyltranstransferase
Gene namesi
Name:Fdps
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68953. Fdps.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: RGD
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075093.
GuidetoPHARMACOLOGYi644.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Farnesyl pyrophosphate synthasePRO_0000123946Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP05369.

PTM databases

iPTMnetiP05369.
PhosphoSiteiP05369.

Expressioni

Tissue specificityi

Testis, liver, kidney, brain and adrenal gland.

Interactioni

Subunit structurei

Homodimer. Interacts with RSAD2 (By similarity).By similarity

Protein-protein interaction databases

MINTiMINT-4575275.

Structurei

3D structure databases

ProteinModelPortaliP05369.
SMRiP05369. Positions 8-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.Curated

Phylogenomic databases

HOGENOMiHOG000160912.
HOVERGENiHBG005741.
InParanoidiP05369.
KOiK00787.
PhylomeDBiP05369.

Family and domain databases

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

P05369-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGDQKLDVH NQEKQNFIQH FSQIVKVLTE DELGHPEKGD AITRIKEVLE
60 70 80 90 100
YNTVGGKYNR GLTVVQTFQE LVEPRKQDAE SLQRALTVGW CVELLQAFFL
110 120 130 140 150
VLDDIMDSSY TRRGQICWYQ KPGIGLDAIN DALLLEAAIY RLLKFYCREQ
160 170 180 190 200
PYYLNLLELF LQSSYQTEIG QTLDLITAPQ GQVDLGRYTE KRYKSIVKYK
210 220 230 240 250
TAFYSFYLPI AAAMYMAGID GEKEHANALK ILLEMGEFFQ IQDDYLDLFG
260 270 280 290 300
DPSVTGKVGT DIQDNKCSWL VVQCLLRATP QQRQILEENY GQKDPEKVAR
310 320 330 340 350
VKALYEELDL RSVFFKYEED SYNRLKSLIE QCSAPLPPSI FLELANKIYK

RRK
Length:353
Mass (Da):40,830
Last modified:February 1, 1991 - v2
Checksum:i27FD7E0DD6FEA001
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101Y → H.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34477 mRNA. Translation: AAA41143.1.
M17300 mRNA. Translation: AAA40960.1. Sequence problems.
BC059125 mRNA. Translation: AAH59125.1.
PIRiA34713.
B34713.
RefSeqiNP_114028.1. NM_031840.1.
UniGeneiRn.2848.

Genome annotation databases

GeneIDi83791.
KEGGirno:83791.
UCSCiRGD:68953. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34477 mRNA. Translation: AAA41143.1.
M17300 mRNA. Translation: AAA40960.1. Sequence problems.
BC059125 mRNA. Translation: AAH59125.1.
PIRiA34713.
B34713.
RefSeqiNP_114028.1. NM_031840.1.
UniGeneiRn.2848.

3D structure databases

ProteinModelPortaliP05369.
SMRiP05369. Positions 8-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4575275.

Chemistry

ChEMBLiCHEMBL1075093.
GuidetoPHARMACOLOGYi644.

PTM databases

iPTMnetiP05369.
PhosphoSiteiP05369.

Proteomic databases

PRIDEiP05369.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi83791.
KEGGirno:83791.
UCSCiRGD:68953. rat.

Organism-specific databases

CTDi2224.
RGDi68953. Fdps.

Phylogenomic databases

HOGENOMiHOG000160912.
HOVERGENiHBG005741.
InParanoidiP05369.
KOiK00787.
PhylomeDBiP05369.

Enzyme and pathway databases

UniPathwayiUPA00259; UER00368.
UPA00260; UER00369.
SABIO-RKP05369.

Miscellaneous databases

NextBioi616373.
PROiP05369.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence of a cholesterol-repressible enzyme related to prenyltransferase in the isoprene biosynthetic pathway."
    Clarke C.F., Tanaka R.D., Svenson K., Wamsley M., Fogelman A.M., Edwards P.A.
    Mol. Cell. Biol. 7:3138-3146(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Testis-specific transcription initiation sites of rat farnesyl pyrophosphate synthetase mRNA."
    Teruya J.H., Kutsunai S.Y., Spear D.H., Edwards P.A., Clarke C.F.
    Mol. Cell. Biol. 10:2315-2326(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
    Strain: Sprague-Dawley.
    Tissue: Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-110.
    Tissue: Pituitary.

Entry informationi

Entry nameiFPPS_RAT
AccessioniPrimary (citable) accession number: P05369
Secondary accession number(s): Q6GT82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 134 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.