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Catalysis of the covalent addition of a geranylgeranyl (20-carbon isoprenoid) group via thioether linkages to a cysteine residue at or near the C terminus of a protein. Catalysis of the reaction: geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate. This reaction is the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. The protein substrates have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine and A2 should not be aromatic. Known substrates include most g-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. Catalysis of the reaction: 2 geranylgeranyl diphosphate + protein-cysteine = 2 S-geranylgeranyl-protein + 2 diphosphate. This reaction is the formation of two thioether linkages between the C-1 atom of the geranylgeranyl groups and two cysteine residues within the terminal sequence motifs XXCC, XCXC or CCXX. Known substrates include Ras-related GTPases of a single family and the Rab family. Catalysis of the covalent addition of an isoprenoid group such as a farnesyl or geranylgeranyl group via thioether linkages to a cysteine residue in a protein. Catalysis of the transfer of a prenyl group from one compound (donor) to another (acceptor).

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein geranylgeranyltransferase activity
Acc: GO:0004661
Aspect: Molecular Function
Desc: Catalysis of the covalent addition of a geranylgeranyl (20-carbon isoprenoid) group via thioether linkages to a cysteine residue at or near the C terminus of a protein.
Synonyms:
  • protein-cysteine geranylgeranyltransferase activity
  • GO:0018224
Proteins in PDR annotated with:
   This term: 6 [Search]
   Term or descendants: 37 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0004661 - protein geranylgeranyltransferase activity (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle