NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1016/S0167-4781(02)00602-4; PubMed=12531482 [NCBI, ExPASy, EBI, Israel, Japan]
Takaya A., Zhang Y.-W., Asawatreratanakul K., Wititsuwannakul D., Wititsuwannakul R., Takahashi S., Koyama T.;
"Cloning, expression and characterization of a functional cDNA clone encoding geranylgeranyl diphosphate synthase of Hevea brasiliensis.";
Biochim. Biophys. Acta 1625:214-220(2003).

[2]

NUCLEOTIDE SEQUENCE [MRNA] OF 165-291.
Bamba T., Nishikawa T., Fukusaki E., Kobayashi A.;
"Prenyltransferase of Hevea brasiliensis.";
Submitted (APR-2000) 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.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=11.5 µM for DMAPP;
	K_M=2.34 µM for GPP;
	K_M=6.78 µM for FPP;
	K_M=24.08 µM for IPP;
	V_max=123 nmol/min/mg enzyme with FPP as substrate;
pH dependence:	Optimum pH is 8.5;
Temperature dependence:	Optimum temperature is 40 degrees Celsius;

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 (Potential).
TISSUE SPECIFICITY: Higher expression in leaves and flowers than in latex and petioles.
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

AB055496; BAB60678.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB041630; BAB16691.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q94ID7; 81-365.

ModBase

Q94ID7.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11666; -.

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 42`	`42`	`Chloroplast (Potential).`
`CHAIN`	`43 370`	`328`	`Geranylgeranyl pyrophosphate synthetase, chloroplastic.`	`PRO_0000045407`
`CONFLICT`	`287 287`		`D -> G (in Ref. 2; BAB16691).`

Sequence information

Length: 370 AA [This is the length of the unprocessed precursor]

Molecular weight: 40096 Da [This is the MW of the unprocessed precursor]

CRC64: F50B10649CE2276E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSVNLGSWV HTSYVLNQAT RSRSKSKSFS LPFNPLKSLA ISFAYRKSER PISSVSAIIT 

        70         80         90        100        110        120 
KEEETLQEEQ NNPPPSFDFK SYMLQKGNSI NQALEAAIPL QEPAKIHESM RYSLLAGGKR 

       130        140        150        160        170        180 
VRPALCLAAC ELVGGNDSMA MPAACAVEMI HTMSLIHDDL PCMDNDDLRR GKPTNHIVFG 

       190        200        210        220        230        240 
EDVAVLAGDA LLAFAFEHIA VSTLNVSSAR IVRAVGELAK AIGAEGLVAG QVVDINSEGS 

       250        260        270        280        290        300 
SEVDLEKLEF IHIHKTAKLL EGAVVLGAIL GGGTDEEVEK LRKYARDIGL LFQVVDDILD 

       310        320        330        340        350        360 
VTKSSQELGK TAGKDLVADK VTYPKLLGIE KSREFAEKLN KEAQEQLAGF DPEKAAPLIA 

       370 
LANYIAHRQN

Q94ID7 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