NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Lamuyo;
TISSUE=Fruit;
PubMed=1303794 [NCBI, ExPASy, EBI, Israel, Japan]
Kuntz M., Roemer S., Suire C., Hugueney P., Weil J.H., Schantz R., Camara B.;
"Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: correlative increase in enzyme activity and transcript level during fruit ripening.";
Plant J. 2:25-34(1992).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Yolo Wonder;
DOI=10.1007/BF00020196; PubMed=7888631 [NCBI, ExPASy, EBI, Israel, Japan]
Badillo A., Steppuhn J., Deruere J., Camara B., Kuntz M.;
"Structure of a functional geranylgeranyl pyrophosphate synthase gene from Capsicum annuum.";
Plant Mol. Biol. 27:425-428(1995).

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 .
SUBUNIT: Monomer.
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

X80267; CAA56554.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S53722; S53722.

3D structure databases

SMR

P80042; 81-369.

ModBase

P80042.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12171; -.

Ontologies

GO:0009536;	Cellular component: plastid (inferred from direct assay from UniProtKB).
GO:0004161;	Molecular function: dimethylallyltranstransferase activity (inferred from direct assay from UniProtKB).
GO:0004311;	Molecular function: farnesyltranstransferase activity (inferred from direct assay from UniProtKB).
GO:0004337;	Molecular function: geranyltranstransferase activity (inferred from direct assay from UniProtKB).
GO:0006720;	Biological process: isoprenoid metabolic process (inferred from direct assay 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.

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 ?`		`Chloroplast.`
`CHAIN`	`? 369`		`Geranylgeranyl pyrophosphate synthetase, chloroplastic.`	`PRO_0000016472`

Sequence information

Length: 369 AA [This is the length of the unprocessed precursor]

Molecular weight: 40173 Da [This is the MW of the unprocessed precursor]

CRC64: 2D527F5E43A29C6F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRSMNLVDLW AQQACLVFNQ TLSYKSFNGF MKIPLKNSKI NPKLNKKRPF SPLTVSAIAT 

        70         80         90        100        110        120 
TKEDERIEAA QTEEPFNFKI YVTEKAISVN KALDEAIIVK EPHVIHEAMR YSLLAGGKRV 

       130        140        150        160        170        180 
RPMLCLAACE LVGGNQENAM AAACAVEMIH TMSLIHDDLP CMDNDDLRRG KPTNHKIYGE 

       190        200        210        220        230        240 
DVAVLAGDSL LAFAFEHIVN STAGVTPSRI VGAVAELAKS IGTEGLVAGQ VADIKCTGNA 

       250        260        270        280        290        300 
SVSLETLEFI HVHKTAALLE SSVVLGAILG GGTNVEVEKL RRFARCIGLL FQVVDDILDV 

       310        320        330        340        350        360 
TKSSEELGKT AGKDLVVDKT TYPKLLGLEK AKEFAAELNR EAKQQLEGFD SRKAAPLIAL 


ADYIAYRDN

P80042 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