[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. TISSUE=Testis; DOI=10.1093/jb/mvh130; PubMed=15598886 [NCBI, ExPASy, EBI, Israel, Japan] Matsumura Y., Kuzuguchi T., Sagami H.; "Relationship between intron 4b splicing of the rat geranylgeranyl diphosphate synthase gene and the active enzyme expression level."; J. Biochem. 136:301-312(2004).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins.
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 .
SUBUNIT: Homooctamer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (Potential).
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

AB118237; BAD30051.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB118238; BAD30052.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB118239; BAD30053.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB118240; BAD30054.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC090327; AAH90327.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001007627.1; -.

UniGene

Rn.54975

3D structure databases

SMR

Q6F596; 6-295.

ModBase

Q6F596.

Organism-specific databases

RGD

1359680; Ggps1.

Gene expression databases

ArrayExpress

Q6F596; -.

GermOnline

ENSRNOG00000016767; Rattus norvegicus.

Ontologies

GO:0005625;	Cellular component: soluble fraction (inferred from sequence or structural similarity from UniProtKB).
GO:0004311;	Molecular function: farnesyltranstransferase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0006720;	Biological process: isoprenoid metabolic process (inferred from sequence or structural similarity from UniProtKB).
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.

Genome annotation databases

Ensembl

ENSRNOG00000016767; Rattus norvegicus. [Contig view]

GeneID

291211; -.

KEGG

rno:291211; -.

NMPDR

fig|10116.3.peg.13440; -.

Phylogenomic databases

HOVERGEN

Q6F596; -.

Other

NextBio

632273; -.

UniRef

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

Keywords

Cytoplasm; Isoprene biosynthesis; Multifunctional enzyme; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 300`	`300`		`Geranylgeranyl pyrophosphate synthetase.`	`PRO_0000123964`

Sequence information

Length: 300 AA [This is the length of the unprocessed precursor]

Molecular weight: 34778 Da [This is the MW of the unprocessed precursor]

CRC64: A3C47E3F9BB81876 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKTKEKAER ILLEPYKYLL QLPGKQVRTK LSQAFNHWLK VPEDKLQIII EVTEMLHNAS 

        70         80         90        100        110        120 
LLIDDIEDSS KLRRGFPVAH SIYGVPSVIN SANYVYFLGL EKVLTLDHPD AVKLFTRQLL 

       130        140        150        160        170        180 
ELHQGQGLDI YWRDTYTCPT EEEYKAMVLQ KTGGLFGLAV GLMQLFSDYK EDLKPLLDTL 

       190        200        210        220        230        240 
GLFFQIRDDY ANLHSKEYSE NKSFCEDLTE GKFSFPTIHA IWSRPESTQV QNILRQRTEN 

       250        260        270        280        290        300 
IDIKKYCVQY LEDVGSFEYT RYTLRELEAK AYKQIEACGG NPSLVALVKH LSKMFTEENE

Q6F596 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