CATH Classification

Domain Context

CATH Clusters

Superfamily Protein prenylyltransferase
Functional Family Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Enzyme Information

2.5.1.58
Protein farnesyltransferase.
based on mapping to UniProt Q04631
Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
-!- This enzyme, along with EC 2.5.1.59 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. -!- These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, gamma-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction.
2.5.1.59
Protein geranylgeranyltransferase type I.
based on mapping to UniProt Q04631
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl- protein + diphosphate.
-!- This enzyme, along with EC 2.5.1.58 and EC 2.5.1.60, constitutes the protein prenyltransferase family of enzymes. -!- Catalyzes 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. -!- These protein acceptors have the C-terminal sequence CA(1)A(2)X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. -!- The enzymes are relaxed in specificity for A(1), but cannot act if A(2) is aromatic. -!- Known targets of this enzyme include most gamma-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. -!- The Zn(2+) is required for peptide, but not for isoprenoid, substrate binding.

UniProtKB Entries (1)

P53610
PGTB1_RAT
Rattus norvegicus
Geranylgeranyl transferase type-1 subunit beta

PDB Structure

PDB 1TNB
External Links
Method X-RAY DIFFRACTION
Organism Spodoptera
Primary Citation
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
Reid, T.S., Terry, K.L., Casey, P.J., Beese, L.S.
J.Mol.Biol.