CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 1 | Mainly Alpha | 
|   | 1.25 | Alpha Horseshoe | 
|   | 1.25.40 | Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat | 
|   | 1.25.40.120 | Protein prenylyltransferase | 
Domain Context
CATH Clusters
| Superfamily | Protein prenylyltransferase | 
| Functional Family | Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha | 
Enzyme Information
| 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. | 
| 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. | 
UniProtKB Entries (1)
| Q02293 | FNTB_RAT Rattus norvegicus Protein farnesyltransferase subunit beta | 
PDB Structure
| PDB | 1X81 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Design, synthesis, and activity of 4-quinolone and pyridone compounds as nonthiol-containing farnesyltransferase inhibitors. Bioorg.Med.Chem.Lett. | 
