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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_2_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 15843: Glutamine amidotransferase, class-II protein

There are 5 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--fructose-6-phosphate transaminase (isomerizing). [EC: 2.6.1.16]
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.
  • Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination).
  • Formerly EC 5.3.1.19.
 296 A0A026V1A6 A0A026V1A6 A0A027U481 A0A027U481 A0A028A655 A0A028A655 A0A028E891 A0A028E891 A0A029IC68 A0A029IC68
(286 more...)
GMP synthase (glutamine-hydrolyzing). [EC: 6.3.5.2]
ATP + XMP + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate.
  • Involved in the de novo biosynthesis of guanosine nucleotides.
  • An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain.
  • The enzyme can catalyze the second reaction alone in the presence of ammonia.
  • Formerly EC 6.3.4.1.
 6 A0A0F4XRJ2 A0A0F4XRJ2 G8PZF6 G8PZF6 Q8EE55 Q8EE55
Amidophosphoribosyltransferase. [EC: 2.4.2.14]
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O.
    		 6 A0A060TB19 A0A060TB19 A0A1C9VMD3 A0A1C9VMD3 A0A1L1PWI6 A0A1L1PWI6
    Gamma-glutamyl hercynylcysteine S-oxide hydrolase. [EC: 3.5.1.118]
    Gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H(2)O = S-(hercyn- 2-yl)-L-cysteine S-oxide + L-glutamate.
    • The enzyme is part of the biosynthesis pathway of ergothioneine in mycobacteria.
    		 2 A0A1C6Z4G0 A0A1C6Z4G0
    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.
    		 2 E4PJ37 E4PJ37
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