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CATH Superfamily 3.40.50.1170

L-asparaginase, N-terminal 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:

"
L-asparaginase, N-terminal 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 1503: Glutamyl-tRNA(Gln) amidotransferase subunit D

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
Asparaginase. [EC: 3.5.1.1]
L-asparagine + H(2)O = L-aspartate + NH(3).
    		 2469 A0A011ASA8 A0A011SHY1 A0A013UIW9 A0A015PBX1 A0A015S893 A0A015SKJ1 A0A015SZ52 A0A015V9P4 A0A015W694 A0A015W877
    (2459 more...)
    Glutamin-(asparagin-)ase. [EC: 3.5.1.38]
    (1) L-glutamine + H(2)O = L-glutamate + NH(3). (2) L-asparagine + H(2)O = L-aspartate + NH(3).
    • L-asparagine is hydrolyzed at 0.8 of the rate of L-glutamine.
    • The D-isomers are also hydrolyzed, more slowly.
    • Cf. EC 3.5.1.1 and EC 3.5.1.2.
    		 233 A0A009GBW4 A0A009HCT2 A0A009HFQ6 A0A009I515 A0A009K4W0 A0A009N6T5 A0A009QCL8 A0A009RT63 A0A009RX70 A0A009SQJ3
    (223 more...)
    Glutathione-disulfide reductase. [EC: 1.8.1.7]
    2 glutathione + NADP(+) = glutathione disulfide + NADPH.
    • Activity is dependent on a redox-active disulfide in each of the active centers.
    • Formerly EC 1.6.4.2.
    		 22 A0A0D6I5V8 A0A0F6B868 A0A0F7JE45 A0A0H3BLB6 A0A0H3NH65 A0A0L3JQY8 A0A0M0QC85 A0A0R9MFI2 A0A0T7RTL0 A0A0U1JX17
    (12 more...)
    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 A0A0W8EAE5 A0A0W8F6Z5 A0A1E3L7L0
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