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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 15582: Proteasome subunit alpha 1

There are 2 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
Proteasome endopeptidase complex. [EC: 3.4.25.1]
Cleavage of peptide bonds with very broad specificity.
  • A 20-S protein composed of 28 subunits arranged in four rings of seven.
  • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
  • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
  • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
  • Terminal apertures restrict access of substrates to the active sites.
  • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
  • Belongs to peptidase family T1.
  • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
 2042 A0A014MUZ0 A0A014MUZ0 A0A021VX80 A0A021VX80 A0A024H2Q5 A0A024H2Q5 A0A024JZY5 A0A024JZY5 A0A024M847 A0A024M847
(2032 more...)
Prokaryotic ubiquitin-like protein ligase. [EC: 6.3.1.19]
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L- lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-like protein]- gamma-L-glutamyl)-[protein]-L-lysine.
  • The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum.
  • It catalyzes the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an epsilon-amino group of a lysine residue of the target protein and the gamma- carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup).
  • The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation.
  • Formerly EC 6.3.2.n2.
 2 A0A0K8QEJ5 A0A0K8QEJ5
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