NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=9288918 [NCBI, ExPASy, EBI, Israel, Japan]
Bonk M., Hoffmann B., von Lintig J., Schledz M., Al-Babili S., Hobeika E., Kleinig H., Beyer P.;
"Chloroplast import of four carotenoid biosynthetic enzymes in vitro reveals differential fates prior to membrane binding and oligomeric assembly.";
Eur. J. Biochem. 247:942-950(1997).

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 stroma (Probable). Plastid, chromoplast (Probable).
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

X98795; CAA67330.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T10452; T10452.

3D structure databases

PDB

2J1O; X-ray; 2.00 A; A=74-366.	[ExPASy / RCSB / EBI]
2J1P; X-ray; 1.80 A; A/B=71-366.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2J1O; -.
2J1P; -.

ModBase

Q43133.

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

3D-structure; Carotenoid biosynthesis; Chloroplast; Chromoplast; Isoprene biosynthesis; Multifunctional enzyme; Plastid; Transferase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 ?`		`Chloroplast and chromoplast.`
`CHAIN`	`? 366`		`Geranylgeranyl pyrophosphate synthetase, chloroplastic/chromoplastic.`	`PRO_0000016474`
`HELIX`	`74 90`	`17`
`HELIX`	`97 108`	`12`
`HELIX`	`114 125`	`12`
`HELIX`	`130 151`	`22`
`HELIX`	`174 195`	`22`
`HELIX`	`202 216`	`15`
`TURN`	`217 219`	`3`
`HELIX`	`221 229`	`9`
`HELIX`	`240 251`	`12`
`HELIX`	`253 266`	`14`
`HELIX`	`271 297`	`27`
`TURN`	`314 316`	`3`
`HELIX`	`319 322`	`4`
`HELIX`	`325 342`	`18`
`TURN`	`343 345`	`3`
`HELIX`	`348 362`	`15`

Sequence information

Length: 366 AA [This is the length of the unprocessed precursor]

Molecular weight: 39432 Da [This is the MW of the unprocessed precursor]

CRC64: 1EADBFD9C4CF4F77 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASSVTPLGS WVLLHHHPST ILTQSRSRSP PSLITLKPIS LTPKRTVSSS SSSSLITKED 

        70         80         90        100        110        120 
NNLKSSSSSF DFMSYIIRKA DSVNKALDSA VPLREPLKIH EAMRYSLLAG GKRVRPVLCI 

       130        140        150        160        170        180 
AACELVGGEE SLAMPARCAV EMIHTMSLIH DDLPCMDNDD LRRGKPTNHK VYGEDVAVLA 

       190        200        210        220        230        240 
GDALLSFAFE HLASATSSEV SPARVVRAVG ELAKAIGTEG LVAGQVVDIS SEGLDLNNVG 

       250        260        270        280        290        300 
LEHLKFIHLH KTAALLEASA VLGGIIGGGS DEEIERLRKF ARCIGLLFQV VDDILDVTKS 

       310        320        330        340        350        360 
SQELGKTAGK DLIADKLTYP KLMGLEKSRE FAEKLNTEAR DQLLGFDSDK VAPLLALANY 


IANRQN

Q43133 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