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:

"
endopeptidase domain like (from Nostoc punctiforme)
".

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.
« Back to all FunFams

FunFam 4: Bifunctional glutathionylspermidine synthetase/ami...

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
Glutathionylspermidine amidase. [EC: 3.5.1.78]
Glutathionylspermidine + H(2)O = glutathione + spermidine.
  • Transforms glutathionylspermidine into glutathione and spermidine.
  • The enzyme from Escherichia coli is bifunctional and also catalyzes the reaction of EC 6.3.1.8, resulting in a net hydrolysis of ATP.
4225 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8
(4215 more...)
Glutathionylspermidine synthase. [EC: 6.3.1.8]
Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate.
  • Involved in the synthesis of trypanothione in trypanosomatids.
  • The enzyme from Escherichia coli is bifunctional and also catalyzes the EC 3.5.1.78 reaction, resulting in a net hydrolysis of ATP.
4225 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8 A0A024LAS8
(4215 more...)
CATH-Gene3D is a Global Biodata Core Resource Learn more...