[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=m567; DOI=10.1007/s004380050477; PubMed=9230902 [NCBI, ExPASy, EBI, Israel, Japan] Mende K., Homann V., Tudzynski B.; "The geranylgeranyl diphosphate synthase gene of Gibberella fujikuroi: isolation and expression."; Mol. Gen. Genet. 255:96-105(1997).

Comments

FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.
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.
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

X96943; CAA65644.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q92236.

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.

Other

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`	`1 418`	`418`	`Geranylgeranyl pyrophosphate synthetase.`	`PRO_0000123965`
`ACT_SITE`	`269 269`		`By similarity.`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 46477 Da [This is the MW of the unprocessed precursor]

CRC64: BE2A0F1EA7D176C9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIPTADPILS FNPEALPPSA LHMLSLSPKA MEKMSGISNP LVSPNAIPPR TSSTGIPTSL 

        70         80         90        100        110        120 
NATPTKPVLR PVPEGDWLSQ KQLSPRAQMS NAGYGVMQAP NPPPDPERYA HEDLEFTAKR 

       130        140        150        160        170        180 
SWTDEKENVV RGPYDYVISH PGKDFRAQLI GAFNVWLDVP TSSLEVITRV VGMLHESSLL 

       190        200        210        220        230        240 
IDDVQDSSEL RRGFPVAHNI FGVAQTINSG NYIYFVALQE LHKLNNPELI TIFSDELVNL 

       250        260        270        280        290        300 
HRGQGMDLFW CDTLTCPTEE DYLEMVGNKT GGLFRLGIKL MAAEANGPSP TDCVPLVNLI 

       310        320        330        340        350        360 
GLIFQIRDDY MNLSSKEYSH NKGMCEDLTE GKFSFPVIHS IRTNPTNLQL INILKQKTSD 

       370        380        390        400        410 
TQIKRYAVAY MESTGSFEYT RKVLSVLIER ARKMAEELDQ GRGSTKGIQK ILDKMAIQ

Q92236 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