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P08836 (FPPS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.

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

Cofactor

Binds 3 magnesium ions per subunit Probable. Ref.2

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. Ref.2 Ref.3

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Farnesyl pyrophosphate synthase
PRO_0000123947

Sites

Metal binding1171Magnesium 1
Metal binding1171Magnesium 2
Metal binding1211Magnesium 1
Metal binding1211Magnesium 2
Metal binding2571Magnesium 3 By similarity
Binding site711Isopentenyl diphosphate By similarity
Binding site741Isopentenyl diphosphate By similarity
Binding site1101Isopentenyl diphosphate By similarity
Binding site1261Dimethylallyl diphosphate
Binding site1271Isopentenyl diphosphate By similarity
Binding site2141Dimethylallyl diphosphate
Binding site2151Dimethylallyl diphosphate By similarity
Binding site2541Dimethylallyl diphosphate By similarity
Binding site2711Dimethylallyl diphosphate By similarity
Binding site2801Dimethylallyl diphosphate
Site1121Important for determining product chain length
Site1131Important for determining product chain length

Experimental info

Mutagenesis1121F → A: Alters selectivity towards product chain length, so that geranylgeranyl diphosphate is produced. Ref.3
Mutagenesis1131F → S: Alters selectivity towards product chain length, so that geranylfarnesyl diphosphate is produced. Ref.3
Sequence conflict1911T → G AA sequence Ref.1
Sequence conflict201 – 2033HFS → TFQ AA sequence Ref.1
Sequence conflict210 – 2123IVK → FVP AA sequence Ref.1
Sequence conflict215 – 2162TA → AM AA sequence Ref.1

Secondary structure

..................................................... 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08836 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: BB23D29D62CD842B

FASTA36742,153
        10         20         30         40         50         60 
MHKFTGVNAK FQQPALRNLS PVVVEREREE FVGFFPQIVR DLTEDGIGHP EVGDAVARLK 

        70         80         90        100        110        120 
EVLQYNAPGG KCNRGLTVVA AYRELSGPGQ KDAESLRCAL AVGWCIELFQ AFFLVADDIM 

       130        140        150        160        170        180 
DQSLTRRGQL CWYKKEGVGL DAINDSFLLE SSVYRVLKKY CRQRPYYVHL LELFLQTAYQ 

       190        200        210        220        230        240 
TELGQMLDLI TAPVSKVDLS HFSEERYKAI VKYKTAFYSF YLPVAAAMYM VGIDSKEEHE 

       250        260        270        280        290        300 
NAKAILLEMG EYFQIQDDYL DCFGDPALTG KVGTDIQDNK CSWLVVQCLQ RVTPEQRQLL 

       310        320        330        340        350        360 
EDNYGRKEPE KVAKVKELYE AVGMRAAFQQ YEESSYRRLQ ELIEKHSNRL PKEIFLGLAQ 


KIYKRQK 

« Hide

References

[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]"Regulation of product chain length by isoprenyl diphosphate synthases."
Tarshis L.C., Proteau P.J., Kellogg B.A., Sacchettini J.C., Poulter C.D.
Proc. Natl. Acad. Sci. U.S.A. 93:15018-15023(1996) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FPSX-ray2.60A20-367[»]
1UBVX-ray2.50A1-367[»]
1UBWX-ray2.50A1-367[»]
1UBXX-ray2.50A1-367[»]
1UBYX-ray2.40A1-367[»]
ProteinModelPortalP08836.
SMRP08836. Positions 20-367.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005741.
PhylomeDBP08836.

Enzyme and pathway databases

UniPathwayUPA00259; UER00368.
UPA00260; UER00369.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
PROSITEPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08836.

Entry information

Entry nameFPPS_CHICK
AccessionPrimary (citable) accession number: P08836
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways