[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan] Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.; "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."; Nature 402:761-768(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=cv. Columbia; DOI=10.1111/j.1467-7652.2006.00183.x; PubMed=17147637 [NCBI, ExPASy, EBI, Israel, Japan] Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.; "Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."; Plant Biotechnol. J. 4:317-324(2006).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 148-304. STRAIN=cv. Wassilewskija; Bartley G.E., Scolnik P.A., Giuliano G.; "Molecular biology of carotenoid biosynthesis in plants."; Plant Physiol. 45:287-301(1994).
[4]	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: Endoplasmic reticulum.
TISSUE SPECIFICITY: Faintly expressed in flowers.
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

AC005724; AAD08933.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006135; AAM15136.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ446521; ABE65826.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L22347; AAA96328.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

G84566; G84566.

NP_179454.1; -.

3D structure databases

SMR

Q9SLG2; 84-367.

ModBase

Q9SLG2.

Enzyme and pathway databases

BioCyc

MetaCyc:AT2G18640-MON; -.

Organism-specific databases

TAIR

At2g18640; -.

Gene expression databases

ArrayExpress

Q9SLG2; -.

Ontologies

GO:0004161;	Molecular function: dimethylallyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004311;	Molecular function: farnesyltranstransferase activity (inferred from electronic annotation from EC).
GO:0004337;	Molecular function: geranyltranstransferase activity (inferred from electronic annotation from EC).
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.

BLOCKS

Q9SLG2.

Genome annotation databases

GeneID

816379; -.

KEGG

ath:AT2G18640; -.

NMPDR

fig|3702.1.peg.8860; -.

Other

ProtoNet

Q9SLG2.

UniRef

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

Keywords

Carotenoid biosynthesis; Complete proteome; Endoplasmic reticulum; Isoprene biosynthesis; Multifunctional enzyme; Signal; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`CHAIN`	`23 372`	`350`	`Geranylgeranyl pyrophosphate synthetase 4.`	`PRO_0000045404`
`CONFLICT`	`152 152`		`I -> M (in Ref. 3; AAA96328).`
`CONFLICT`	`303 303`		`E -> V (in Ref. 3; AAA96328).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 40936 Da [This is the MW of the unprocessed precursor]

CRC64: C16F7F798BB7051A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAQNIFLYL LIVFLSLHFV FTTLKGRLSP ANTRRLIRLL HIPIKSPVAA AIFARKDTRE 

        70         80         90        100        110        120 
FLDSSIKLVN EEDDFGFSFD FKPYMISKAE TINRALDEAI PLIEPLNIHK AMRYAILAGG 

       130        140        150        160        170        180 
KRVRPILCLA ACELVGGEER LAIQAACAVE MIHTMSLIKD DLPCMDNDDL RRGKPTTHKV 

       190        200        210        220        230        240 
FGESVAILSG GALLALAFEH LTEADVSSKK MVRAVKELAK SIGTKGLVAG QAKDLSSEGL 

       250        260        270        280        290        300 
EQNDVGLEDL EYIHVHKTGS LLEASAVIGA VIGGGTEKEI EKVRNFARCI GLLFQVVDDI 

       310        320        330        340        350        360 
LDETKSSEEL GKTAGKDKVA GKLTYPKVIG VEKSKEFVEK LKRDAREHLQ GFDSDKVKPL 

       370 
IALTNFIANR NH

Q9SLG2 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