NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=m567;
DOI=10.1007/s002940050126; PubMed=8753652 [NCBI, ExPASy, EBI, Israel, Japan]
Homann V., Mende K., Arntz C., Ilardi V., Macino G., Morelli G., Bose G., Tudzynski B.;
"The isoprenoid pathway: cloning and characterization of fungal FPPS genes.";
Curr. Genet. 30:232-239(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.
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

X96940; CAA65641.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S71435; S71435.

3D structure databases

HSSP

P08836; 1UBX. [HSSP ENTRY / PDB]

ModBase

Q92235.

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`	`1 347`	`347`	`Farnesyl pyrophosphate synthetase.`	`PRO_0000123948`
`ACT_SITE`	`184 184`		`By similarity.`

Sequence information

Length: 347 AA [This is the length of the unprocessed precursor]

Molecular weight: 40236 Da [This is the MW of the unprocessed precursor]

CRC64: DC39B016658441E4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQQTTLQEF NSVYPKLEEA LLDHARSYKL PQEQLDWYKR SLEVNPLGGK CNRGMSVPDS 

        70         80         90        100        110        120 
VSLLLEKPLT EEQYFQAATL GWMTELLQAF FLVSDDIMDS SITRRGQPCW YRQEGVGMIA 

       130        140        150        160        170        180 
INDAFMLESA IYTLLKKYFR SHPAYFDLIE SFHETTFQTE LGQLCDLLTA PEDNVNLDNF 

       190        200        210        220        230        240 
SLEKYSFIVI YKTAYYSFYL PVALALHQLN LATPSNLKQA EDILIPLGEY FQIQDDYLDN 

       250        260        270        280        290        300 
FGKPEHIGKI GTDIKDNKCS WLVNQALAVA TPEQRKILEE NYGRKDDEKE KVVKKLYDDL 

       310        320        330        340 
NLEQRYLDYE EKVVGQIRER IANIDENDGL KKTVFEAFLA KIYKRSK

Q92235 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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