[1]	NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. STRAIN=cv. Landsberg erecta; DOI=10.1023/A:1005898805326; PubMed=9349257 [NCBI, ExPASy, EBI, Israel, Japan] Zhu X., Suzuki K., Saito T., Okada K., Tanaka K., Nakagawa T., Matsuda H., Kawamukai M.; "Geranylgeranyl pyrophosphate synthase encoded by the newly isolated gene GGPS6 from Arabidopsis thaliana is localized in mitochondria."; Plant Mol. Biol. 35:331-341(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION. 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).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan] Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; Nature 408:816-820(2000).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.; Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.

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: Mitochondrion.
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

AB000835; BAA23157.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007504; AAD43148.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT011230; AAR92266.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT012158; AAS76253.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_175376.1; -.

UniGene

At.38214

3D structure databases

ModBase

O22043.

Organism-specific databases

TAIR

At1g49530; -.

Gene expression databases

GermOnline

AT1G49530; 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

O22043.

Genome annotation databases

GeneID

841377; -.

GenomeReviews

CT485782_GR; AT1G49530.

KEGG

ath:AT1G49530; -.

NMPDR

fig|3702.1.peg.4426; -.

Other

ProtoNet

O22043.

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 22`	`22`	`Mitochondrion (Potential).`
`CHAIN`	`23 336`	`314`	`Geranylgeranyl pyrophosphate synthetase 6, mitochondrial.`	`PRO_0000045405`
`CONFLICT`	`1 1`		`M -> MLCKIIIM (in Ref. 1 and 2).`
`CONFLICT`	`4 4`		`R -> C (in Ref. 1 and 2).`
`CONFLICT`	`8 8`		`I -> V (in Ref. 1 and 2).`
`CONFLICT`	`37 37`		`K -> N (in Ref. 1 and 2).`
`CONFLICT`	`57 57`		`F -> S (in Ref. 1 and 2).`
`CONFLICT`	`77 77`		`P -> S (in Ref. 1 and 2).`
`CONFLICT`	`133 133`		`K -> I (in Ref. 1 and 2).`
`CONFLICT`	`153 153`		`R -> M (in Ref. 1 and 2).`

Sequence information

Length: 336 AA [This is the length of the unprocessed precursor]

Molecular weight: 36886 Da [This is the MW of the unprocessed precursor]

CRC64: 95F32D360003C954 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRPRYSLILS AMRLIRPSNR RLSSIASSDS EFISYMKNKA KSINKALDNS IPLCNNFVPL 

        70         80         90        100        110        120 
WEPVLEVHKA MRYTLLPGGK RVRPMLCLVA CELVGGQEST AMPAACAVEM IHAASLILDD 

       130        140        150        160        170        180 
LPCMDDDSLR RGKPTNHKVF GEKTSILASN ALRSLAVKQT LASTSLGVTS ERVLRAVQEM 

       190        200        210        220        230        240 
ARAVGTEGLV AGQAADLAGE RMSFKNEDDE LRYLELMHVH KTAVLVEAAA VVGAIMGGGS 

       250        260        270        280        290        300 
DEEIERLKSY ARCVGLMFQV MDDVLDETKS SEELGKTAGK DLITGKLTYP KVMGVDNARE 

       310        320        330 
YAKRLNREAQ EHLQGFDSDK VVPLLSLADY IVKRQN

O22043 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