The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Amidase signature (AS) domain
".

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 1834: Glutamyl-tRNA(Gln) amidotransferase subunit A

There are 1 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
Glutaminyl-tRNA synthase (glutamine-hydrolyzing). [EC: 6.3.5.7]
ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
  • In systems lacking discernible EC 6.1.1.18, glutaminyl-tRNA(Gln) is formed by a two-enzyme system.
  • In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln).
  • The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl- tRNA(Glu) is not a substrate for this reaction).
  • Ammonia or asparagine can substitute for the preferred substrate glutamine.
208 A0A023P0J2 A0A068N598 A0A076W954 A0A084IXV7 A0A090Z694 A0A0B5NS98 A0A0B5P2F8 A0A0B5R5A9 A0A0B5RZA5 A0A0B5ZC88
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