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CATH Superfamily 3.90.1300.10

Amidase signature (AS) domain

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 546: Glutamyl-tRNA(Gln) amidotransferase subunit A

There are 4 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
Amidase. [EC: 3.5.1.4]
A monocarboxylic acid amide + H(2)O = a monocarboxylate + NH(3).
    		 8 A0A0F4Z245 A0A0F8B4E8 A0A0J6S1L7 A0A0Q0T077 A0A171A654 G4VCJ2 P08158 Q12559
    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.
    		 3 A0A060RTA6 A0A0D2FYS8 Q8I1S6
    Mandelamide amidase. [EC: 3.5.1.86]
    (R)-mandelamide + H(2)O = (R)-mandelate + NH(3).
      		 2 A0A0D1JU28 A0A0D1KAY4
      Allophanate hydrolase. [EC: 3.5.1.54]
      Urea-1-carboxylate + H(2)O = 2 CO(2) + 2 NH(3).
      • Along with EC 3.5.2.15 and EC 3.5.1.84, forms part of the cyanuric- acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine (2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5- triazine), in bacteria.
      • The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 6.3.4.6, thus bringing about the hydrolysis of urea to CO(2) and NH(3) in the presence of ATP and bicarbonate.
      • The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate.
      		 1 A0A087E8U4