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Q8WMY2 (FPPS_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Farnesyl pyrophosphate synthase
Short name=FPP synthase
Short name=FPS
EC=2.5.1.10
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase
Dimethylallyltranstransferase
EC=2.5.1.1
Farnesyl diphosphate synthase
Geranyltranstransferase
Gene names
Name:FDPS
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.

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

Cofactor

Binds 3 magnesium ions per subunit By similarity.

Enzyme regulation

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 envelopped viruses need lipid rafts to bud efficiently out of the cell By similarity.

Pathway

Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.

Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.

Subunit structure

Homodimer. Interacts with RSAD2 By similarity. Interacts with bovine leukemia virus (BLV) protein G4. Ref.1

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 353353Farnesyl pyrophosphate synthase
PRO_0000237610

Sites

Metal binding1031Magnesium 1 By similarity
Metal binding1031Magnesium 2 By similarity
Metal binding1071Magnesium 1 By similarity
Metal binding1071Magnesium 2 By similarity
Metal binding2431Magnesium 3 By similarity
Binding site571Isopentenyl diphosphate By similarity
Binding site601Isopentenyl diphosphate By similarity
Binding site961Isopentenyl diphosphate By similarity
Binding site1121Dimethylallyl diphosphate By similarity
Binding site1131Isopentenyl diphosphate By similarity
Binding site2001Dimethylallyl diphosphate By similarity
Binding site2011Dimethylallyl diphosphate By similarity
Binding site2401Dimethylallyl diphosphate By similarity
Binding site2571Dimethylallyl diphosphate By similarity
Binding site2661Dimethylallyl diphosphate By similarity
Site981Important for determining product chain length By similarity
Site991Important for determining product chain length By similarity

Amino acid modifications

Modified residue571N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8WMY2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 6FCAA8526E0826BE

FASTA35340,510
        10         20         30         40         50         60 
MNGDQKLDAY AQERQDFIQH FSQIVKVLTE EDIGHPEIGD AITRLKEVLE YNAIGGKYNR 

        70         80         90        100        110        120 
GLTVVITFRE LVEPGKQDPD SLQRALTVGW CVELLQAFFL VSDDIMDSSL TRRGQTCWYQ 

       130        140        150        160        170        180 
KPGIGLDAIN DAFLLESSIY RLLKLYCREQ PYYLDLIELF LQSSYQTEIG QTLDLITAPQ 

       190        200        210        220        230        240 
GNVDLGRFTE KRYKSIVKYK TAFYSFYLPV AAAMYMAGID GEKEHAHAKK ILLEMGEFFQ 

       250        260        270        280        290        300 
IQDDYLDLFG DPSMTGKIGT DIQDNKCSWL VVQCLQRASP EQRQILQENY GQKEAEKVAR 

       310        320        330        340        350 
VKALYEEMNL SAVYMQYEED SYNHIMGLIE QYAAPLPPAI FLGLAQKIYK RKK

« Hide

References

« Hide 'large scale' references
[1]"Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 p13(II) accessory proteins interact with farnesyl pyrophosphate synthetase."
Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H., Dangoisse O., Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A., Kettmann R., Willems L.
J. Virol. 76:1400-1414(2002) [PubMed: 11773414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BLV G4.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF461050 mRNA. Translation: AAL58886.1.
BC149572 mRNA. Translation: AAI49573.1.
IPIIPI00839514.
RefSeqNP_803463.1. NM_177497.2.
UniGeneBt.23182.

3D structure databases

ProteinModelPortalQ8WMY2.
SMRQ8WMY2. Positions 8-353.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8WMY2.

Proteomic databases

PRIDEQ8WMY2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281156.
KEGGbta:281156.

Organism-specific databases

CTD2224.

Phylogenomic databases

eggNOGmaNOG15674.
GeneTreeENSGT00530000063878.
HOVERGENHBG005741.
PhylomeDBQ8WMY2.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
KOK00787.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. Terpenoid_synth. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPPS_BOVIN
AccessionPrimary (citable) accession number: Q8WMY2
Secondary accession number(s): A6QPZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2002
Last modified: November 16, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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