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CATH Superfamily 3.60.20.10

Aminohydrolase, N-terminal nucleophile (Ntn) domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
".

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 24: Asparagine synthetase [glutamine-hydrolyzing]

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
Asparagine synthase (glutamine-hydrolyzing). [EC: 6.3.5.4]
ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate.
  • The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel.
  • The enzyme catalyzes three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain.
  • The C-terminal active site mediates both the synthesis of a beta- aspartyl-AMP intermediate and its subsequent reaction with ammonia.
  • The ammonia released is channeled to the other active site to yield asparagine.
 24 A0A178U7S3 A0A178U7S3 A0A178VBT4 A0A178VBT4 B8B0C7 B8B0C7 B8B0C7 P19251 P49078 P49078
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