NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51;
DOI=10.1126/science.1095781; PubMed=15001715 [NCBI, ExPASy, EBI, Israel, Japan]
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.;
"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome.";
Science 304:304-307(2004).

Comments

FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. May be involved in vesicle trafficking and protein sorting (By similarity).
CATALYTIC ACTIVITY: Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate.
CATALYTIC ACTIVITY: Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.
CATALYTIC ACTIVITY: Trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl 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 .
PATHWAY: Isoprenoid biosynthesis; geranylgeranyl-PP biosynthesis; geranylgeranyl-PP from farnesyl-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

AE016818; AAS52447.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_984623.1; -.

3D structure databases

ModBase

Q758K0.

Organism-specific databases

AGD

AEL238C; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004161;	Molecular function: dimethylallyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004311;	Molecular function: farnesyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004337;	Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
GO:0016117;	Biological process: carotenoid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0015031;	Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000092; Polyprenyl_synt.
IPR017446; Polyprenyl_synth-rel.
IPR008949; Terpenoid_synth.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.600.10; Terpenoid_synth; 1.

PANTHER

PTHR12001; Polyprenyl_synt; 1.

Pfam

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

PROSITE

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

ProtoNet

Q758K0.

Genome annotation databases

4620805; -.

fig|33169.1.peg.2268; -.

Phylogenomic databases

HOGENOM

Q758K0; -.

Other

UniRef

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

Keywords

Carotenoid biosynthesis; Complete proteome; Cytoplasm; Isoprene biosynthesis; Multifunctional enzyme; Protein transport; Transferase; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 320`	`320`	`Geranylgeranyl pyrophosphate synthetase.`	`PRO_0000228138`
`ACT_SITE`	`168 168`		`By similarity.`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 35984 Da [This is the MW of the unprocessed precursor]

CRC64: EFA9BE35C2F831BF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDSVEGLALG PVIWTASQEE LLRQPYNHLV TQPGKNFRNT LIRVFNGFYG LSERQVAAVT 

        70         80         90        100        110        120 
ELVEMLHVAS LLIDDIEDNS AWRRGVAAAH VVYGSPMTIN TANYMYFVSM SLLGQLAAQR 

       130        140        150        160        170        180 
PAGPLQDLLK VFNEEMMNLH RGQGLDIYWR DTFTVPSEHD YLRMVMHKTG GLFRLTVRIM 

       190        200        210        220        230        240 
EALREGPDGP GSTLVPLSNL LGVLYQVRDD YLNLTDSRMS ENKGFADDIT EGKFSYPIIH 

       250        260        270        280        290        300 
GLQYARVHDP AGYDFLVSVL RQRTTDITTK RRVVRYLADV SGSLAYTKQR IIELATLIKT 

       310        320 
KYIPASGTEL CNVIDSLTSF

Q758K0 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