CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.50 | Alpha/alpha barrel | |
1.50.10 | Glycosyltransferase | |
1.50.10.20 |
Domain Context
CATH Clusters
Superfamily | 1.50.10.20 |
Functional Family | Protein farnesyltransferase subunit beta |
Enzyme Information
2.5.1.58 |
Protein farnesyltransferase.
based on mapping to UniProt P49356
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.
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UniProtKB Entries (1)
P49354 |
FNTA_HUMAN
Homo sapiens
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
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PDB Structure
PDB | 2IEJ |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase.
Mol.Biochem.Parasitol.
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