[1]	PROTEIN SEQUENCE OF 187-216. TISSUE=Liver; DOI=10.1021/bi00516a007; PubMed=7272273 [NCBI, ExPASy, EBI, Israel, Japan] Brems D.N., Bruenger E., Rillings H.C.; "Isolation and characterization of a photoaffinity-labeled peptide from the catalytic site of prenyltransferase."; Biochemistry 20:3711-3718(1981).
[2]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-367. TISSUE=Liver; DOI=10.1021/bi00202a004; PubMed=8086404 [NCBI, ExPASy, EBI, Israel, Japan] Tarshis L.C., Yan M., Poulter C.D., Sacchettini J.C.; "Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution."; Biochemistry 33:10871-10877(1994).
[3]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-367. TISSUE=Liver; DOI=10.1073/pnas.93.26.15018; PubMed=8986756 [NCBI, ExPASy, EBI, Israel, Japan] Tarshis L.C., Proteau P.J., Kellogg B.A., Sacchettini J.C., Poulter C.D.; "Regulation of product chain length by isoprenyl diphosphate synthases."; Proc. Natl. Acad. Sci. U.S.A. 93:15018-15023(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 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
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

UniGene

Gga.42725

3D structure databases

PDB

1FPS; X-ray; 2.60 A; A=20-367.	[ExPASy / RCSB / EBI]
1UBV; X-ray; 2.50 A; A=1-367.	[ExPASy / RCSB / EBI]
1UBW; X-ray; 2.50 A; A=1-367.	[ExPASy / RCSB / EBI]
1UBX; X-ray; 2.50 A; A=1-367.	[ExPASy / RCSB / EBI]
1UBY; X-ray; 2.40 A; A=1-367.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FPS; -.
1UBV; -.
1UBW; -.
1UBX; -.
1UBY; -.

ModBase

P08836.

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.

BLOCKS

P08836.

Phylogenomic databases

HOGENOM

P08836; -.

HOVERGEN

P08836; -.

Other

P08836; -.

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

Keywords

3D-structure; Cholesterol biosynthesis; Cytoplasm; Direct protein sequencing; Isoprene biosynthesis; Lipid synthesis; Steroid biosynthesis; Sterol biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`Farnesyl pyrophosphate synthetase.`	`PRO_0000123947`
`ACT_SITE`	`206 206`
`CONFLICT`	`191 191`		`T -> G (in Ref. 1; AA sequence).`
`CONFLICT`	`201 203`		`HFS -> TFQ (in Ref. 1; AA sequence).`
`CONFLICT`	`210 212`		`IVK -> FVP (in Ref. 1; AA sequence).`
`CONFLICT`	`215 216`		`TA -> AM (in Ref. 1; AA sequence).`
`HELIX`	`21 33`	`13`
`HELIX`	`35 43`	`9`
`TURN`	`44 46`	`3`
`TURN`	`50 52`	`3`
`HELIX`	`53 66`	`14`
`STRAND`	`67 70`	`4`
`HELIX`	`73 85`	`13`
`HELIX`	`88 90`	`3`
`HELIX`	`93 121`	`29`
`HELIX`	`132 134`	`3`
`TURN`	`136 140`	`5`
`HELIX`	`141 161`	`21`
`HELIX`	`167 191`	`25`
`HELIX`	`204 214`	`11`
`HELIX`	`216 219`	`4`
`HELIX`	`221 231`	`11`
`HELIX`	`236 263`	`28`
`STRAND`	`276 278`	`3`
`HELIX`	`283 291`	`9`
`HELIX`	`294 303`	`10`
`HELIX`	`309 322`	`14`
`HELIX`	`324 346`	`23`
`STRAND`	`348 350`	`3`
`HELIX`	`353 362`	`10`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 42153 Da [This is the MW of the unprocessed precursor]

CRC64: BB23D29D62CD842B [This is a checksum on the sequence]

        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

P08836 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