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Reviewed, UniProtKB/Swiss-Prot Q43133 (GGPPS_SINAL)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Geranylgeranyl pyrophosphate synthetase, chloroplastic/chromoplastic
      Short name=GGPP synthetase
      Short name=GGPS
Including the following 3 domains:
    1- Recommended name:
            Dimethylallyltranstransferase
              EC=2.5.1.1
    2- Recommended name:
            Geranyltranstransferase
              EC=2.5.1.10
    3- Recommended name:
            Farnesyltranstransferase
              EC=2.5.1.29
Gene names
Name: GGPS1
Synonyms: GGPS
OrganismSinapis alba (White mustard) (Brassica hirta)
Taxonomic identifier3728 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeSinapis

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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.

Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate.

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.

Isoprenoid biosynthesis; geranyl-PP biosynthesis; geranyl-PP from dimethylallyl-PP and isopentenyl-PP: step 1/1.

Isoprenoid biosynthesis; geranylgeranyl-PP biosynthesis; geranylgeranyl-PP from farnesyl-PP and isopentenyl-PP: step 1/1.

Subunit structure

Monomer.

Subcellular location

Plastidchloroplast stroma Probable. Plastidchromoplast Probable.

Sequence similarities

Belongs to the FPP/GGPP synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast and chromoplast
Chain? – 366Geranylgeranyl pyrophosphate synthetase, chloroplastic/chromoplasticPRO_0000016474

Secondary structure

............................... 366
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q43133-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 1EADBFD9C4CF4F77

FASTA36639,432
        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 

« Hide

References

[1]"Chloroplast import of four carotenoid biosynthetic enzymes in vitro reveals differential fates prior to membrane binding and oligomeric assembly."
Bonk M., Hoffmann B., von Lintig J., Schledz M., Al-Babili S., Hobeika E., Kleinig H., Beyer P.
Eur. J. Biochem. 247:942-950(1997) [PubMed: 9288918] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

X98795 mRNA. Translation: CAA67330.1.
PIRT10452.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2J1OX-ray2.00A74-366[»]
2J1PX-ray1.80A/B74-366[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.5.1.1. 20822.
2.5.1.10. 20822.
2.5.1.29. 20822.

Family and domain databases

InterProIPR000092. Polyprenyl_synt.
IPR017446. Polyprenyl_synth-rel.
IPR008949. Terpenoid_synth.
[Graphical view]
Gene3DG3DSA:1.10.600.10. Terpenoid_synth. 1 hit.
PANTHERPTHR12001. Polyprenyl_synt. 1 hit.
PfamPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
PROSITEPS00723. POLYPRENYL_SYNTHET_1. 1 hit.
PS00444. POLYPRENYL_SYNTHET_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGGPPS_SINAL
AccessionPrimary (citable) accession number: Q43133
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents