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CATH Superfamily 1.20.120.330

Nucleotidyltransferases domain 2

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:

"
Nucleotidyltransferases domain 2
".

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 34: Bifunctional glutamine synthetase adenylyltransfer...

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
[Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase. [EC: 2.7.7.89]
[Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP.
  • This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2.
  • The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42).
  • The two activities are present on separate domains.
  • Formerly EC 3.1.4.15.
 4 A0A0E4G0H4 A0A0E4G0H4 Q89QJ5 Q89QJ5
[Glutamine synthetase] adenylyltransferase. [EC: 2.7.7.42]
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine.
  • This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2.
  • The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89).
  • The two activities are present on separate domains.
 4 A0A0E4G0H4 A0A0E4G0H4 Q89QJ5 Q89QJ5
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