[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. G. Don c20; Bantignies B., Liboz T., Ambid C.; "Nucleotide sequence of a Catharanthus roseus geranylgeranyl pyrophosphate synthase gene."; (er) Plant Gene Register PGR95-119.

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: Plastid, chloroplast.
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

X92893; CAA63486.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T09966; T09966.

3D structure databases

SMR

Q42698; 68-352.

ModBase

Q42698.

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

Carotenoid biosynthesis; Chloroplast; Isoprene biosynthesis; Multifunctional enzyme; Plastid; Transferase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 40`	`40`	`Chloroplast (Potential).`
`CHAIN`	`41 357`	`317`	`Geranylgeranyl pyrophosphate synthetase, chloroplastic.`	`PRO_0000016473`

Sequence information

Length: 357 AA [This is the length of the unprocessed precursor]

Molecular weight: 38787 Da [This is the MW of the unprocessed precursor]

CRC64: 81C52FDEA1E06FA8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRSNLCHPLK NQLPISFFLS GTIRKPIFSC SRLSISAIIT KEQTQEESES KSKKEVAFSS 

        70         80         90        100        110        120 
SSSFDFKAYM IGKANSVNKA LEDAVLVREP LKIHESMRYS LLAGGKRVRP MLCIAACELF 

       130        140        150        160        170        180 
GGTESVAMPS ACAVEMIHTM SLMHDDLPCM DNDDLRRGKP TNHKVFGEDV AVLAGDALLA 

       190        200        210        220        230        240 
FAFEHIATAT KGVSSERIVR VVGELAKCIG SEGLVAGQVV DVCSEGIADV GLEHLEFIHI 

       250        260        270        280        290        300 
HKTAALLEGS VVLGAIVGGA NDEQISKLRK FARCIGLLFQ VVDDILDVTK SSQELGKTAG 

       310        320        330        340        350 
KDLVADKVTY PKLLGIDKSR EFAEKLNREA QEQLAEFDPE KAAPLIALAN YIAYRDN

Q42698 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