NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Root;
DOI=10.1006/abbi.1995.1422; PubMed=7646076 [NCBI, ExPASy, EBI, Israel, Japan]
Attucci S., Aitken S.M., Gulick P.J., Ibrahim R.K.;
"Farnesyl pyrophosphate synthase from white lupin: molecular cloning, expression, and purification of the expressed protein.";
Arch. Biochem. Biophys. 321:493-500(1995).

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 (By similarity).
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

U20771; AAA87729.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S66471; S66471.

3D structure databases

HSSP

P08836; 1UBY. [HSSP ENTRY / PDB]

ModBase

P49352.

Ontologies

GO:0004161;	Molecular function: dimethylallyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004337;	Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
QuickGo view.

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 2.`	`PRO_0000123957`

Sequence information

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

Molecular weight: 39311 Da [This is the MW of the unprocessed precursor]

CRC64: EB2C3AD89626E42D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADPKSSFLN VYSILKSELL QDPAFEFSTD SRQWVERMLD YNVPGGKLNR GLSVIDSYKL 

        70         80         90        100        110        120 
LKDGQELNDE EIFLASALGW CIEWLQAYFL VLDDIMDNSH TRRGHPCWFR VPKVGMIAPN 

       130        140        150        160        170        180 
DGVVLRNHIP RILKKHFRGK PYYVDLLDLF NEVEFQTASG QMIDLITTLE GEKDLSKYTL 

       190        200        210        220        230        240 
SLHRRIVQYK TAYYSFYLPV ACALLMVGEN LDNHTDVKNI LVEMGTYFQV QDDYLDCFGA 

       250        260        270        280        290        300 
PETIGKIGTD IEDFKCSWLV VKALELSNEE QKKVLYENYG KPDPANVAKV KTLYNELNLE 

       310        320        330        340 
GAYADYESKS YEKLVTCIEG HPSKAVQGVL KSFWAKIYKR QK

P49352 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