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CATH Superfamily 1.25.40.120

Protein prenylyltransferase

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Protein prenylyltransferase
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 9: CAAX geranylgeranyltransferase alpha subunit

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Protein geranylgeranyltransferase type I. [EC: 2.5.1.59]
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.
 90 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A1D8PEN1
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Protein farnesyltransferase. [EC: 2.5.1.58]
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.
 90 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A0L8VMQ3 A0A1D8PEN1
(80 more...)
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