NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Line 11591;
TISSUE=Stem bark;
DOI=10.1006/abbi.1996.0333; PubMed=8806726 [NCBI, ExPASy, EBI, Israel, Japan]
Pan Z., Herickhoff L.A., Backhaus R.A.;
"Cloning, characterization, and heterologous expression of cDNAs for farnesyl diphosphate synthase from the guayule rubber plant reveals that this prenyltransferase occurs in rubber particles.";
Arch. Biochem. Biophys. 332:196-204(1996).

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.
CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.
PATHWAY: Isoprenoid biosynthesis; farnesyl-PP biosynthesis; farnesyl-PP from geranyl-PP and isopentenyl-PP: step 1/1 .
PATHWAY: Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1 .
SUBCELLULAR LOCATION: Cytoplasm. Note=Rubber particles.
SIMILARITY: Belongs to the FPP/GGPP synthetase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X82542; CAA57892.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S71398; S71398.

3D structure databases

HSSP

P08836; 1UBY. [HSSP ENTRY / PDB]

ModBase

O24241.

Family and domain databases

InterPro

IPR000092; Polyprenyl_synt.
IPR008949; Terpenoid_synth.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.600.10; Terpenoid_synth; 1.

Pfam

PF00348; polyprenyl_synt; 1.
Pfam graphical view of domain structure.

PROSITE

PS00723; POLYPRENYL_SYNTHET_1; 1.
PS00444; POLYPRENYL_SYNTHET_2; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cholesterol biosynthesis; Cytoplasm; Isoprene biosynthesis; Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 342`	`342`		`Farnesyl pyrophosphate synthetase 1.`	`PRO_0000123959`

Sequence information

Length: 342 AA [This is the length of the unprocessed precursor]

Molecular weight: 39367 Da [This is the MW of the unprocessed precursor]

CRC64: D49AA182B74ED6EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSDLKSRFL QVYDTLKSEL INDPAFEFDD DSRQWVEKML DYNVPGGKLN RGLSVIDSYQ 

        70         80         90        100        110        120 
LLKGGELTDN EIFLAAALGW CIEWLQAYFL VLDDIMDESH TRRGQPCWFR LPKVGMIAAN 

       130        140        150        160        170        180 
DGIILRNNVP RILKKHFRGK PYYVDLLDLF NEVEFQTASG QMIDLITTLV GEKDLSKYSL 

       190        200        210        220        230        240 
SIHRRIVQYK TAYYSFYLPV ACALLMFGED LEKHEEVKNV LVEMGTYFQV QDDYLDCFGA 

       250        260        270        280        290        300 
PEVIGKIGTD IEDFKCSWLV VKALELSNEE QKKILHENYG KKDPSSVAKV KELYHTLNLQ 

       310        320        330        340 
GVFEDYENTS YKKLITSIEG HPSKAVQAVL KSFLGKIYKR QK

O24241 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools