[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/7.2.131; PubMed=10819329 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."; DNA Res. 7:131-135(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan] Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.; "Functional annotation of a full-length Arabidopsis cDNA collection."; Science 296:141-145(2002).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.; "Full-length cDNA from Arabidopsis thaliana."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 139-360. STRAIN=cv. Landsberg erecta; TISSUE=Flower; Scolnik P.A., Bartley G.E.; "Two more members of an Arabidopsis geranylgeranyl pyrophosphate synthase gene family."; (er) Plant Gene Register PGR96-014.
[5]	SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1104/pp.122.4.1045; PubMed=10759500 [NCBI, ExPASy, EBI, Israel, Japan] Okada K., Saito T., Nakagawa T., Kawamukai M., Kamiya Y.; "Five geranylgeranyl diphosphate synthases expressed in different organs are localized into three subcellular compartments in Arabidopsis."; Plant Physiol. 122:1045-1056(2000).

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 (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
TISSUE SPECIFICITY: Mainly expressed in roots.
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

AB023038; BAB02387.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK117933; BAC42571.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086932; AAM64496.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U44877; AAB67731.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S71231; S71231.

UniGene

At.22423

3D structure databases

SMR

Q9LUD9; 69-355.

ModBase

Q9LUD9.

Organism-specific databases

TAIR

At3g14550; -.

Gene expression databases

GermOnline

AT3G14550; Arabidopsis thaliana.

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.

BLOCKS

Q9LUD9.

Genome annotation databases

GenomeReviews

BA000014_GR; AT3G14550.

NMPDR

fig|3702.1.peg.13594; -.

Other

ProtoNet

Q9LUD9.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 39`	`39`	`Chloroplast (Potential).`
`CHAIN`	`40 360`	`321`	`Geranylgeranyl pyrophosphate synthetase 3, chloroplastic.`	`PRO_0000045403`
`CONFLICT`	`8 8`		`S -> N (in Ref. 2; BAC42571).`
`CONFLICT`	`55 55`		`G -> R (in Ref. 3; AAM64496).`
`CONFLICT`	`209 209`		`A -> T (in Ref. 2; BAC42571).`
`CONFLICT`	`289 289`		`L -> P (in Ref. 3; AAM64496).`
`CONFLICT`	`328 328`		`K -> E (in Ref. 3; AAM64496).`
`CONFLICT`	`354 354`		`Y -> H (in Ref. 4; AAB67731).`
`CONFLICT`	`357 357`		`C -> F (in Ref. 4; AAB67731).`

Sequence information

Length: 360 AA [This is the length of the unprocessed precursor]

Molecular weight: 38844 Da [This is the MW of the unprocessed precursor]

CRC64: FDB5244FCBBB2742 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATTVHLSSF SLFIQSRGRR DNSISSVKSL KKRTGLSPSS ALTSQGGRDM IPPEGKCNDH 

        70         80         90        100        110        120 
NSAFDFKLYM IRKAESVNAA LDVSVPLREP LTVQEAVRYS LLAGGKRVRP LLCIAVCELV 

       130        140        150        160        170        180 
GGDEATAMSA ACAVEMIHTS SLIHDDLPCM DNADLRRGKP TNHKVYGEDM AVLAGDALLA 

       190        200        210        220        230        240 
LAFEHMTVVS SGLVAPERMI RAVVELARAI GTTGLVAGQM IDLASERLNP DKVGLEHLEF 

       250        260        270        280        290        300 
IHLHKTAALL EAAAVLGVIM GGGTEEEIEK LRKYARCIGL LFQVVDDILD VTKSTEELGK 

       310        320        330        340        350        360 
TAGKDVMAGK LTYPRLIGLE RSKEVAEKLR REAEEQLLGF DPSKAAPLVA LASYIACRHN

Q9LUD9 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