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 15813: Proteasome subunit beta type

There are 6 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.
5658 A0A010RB16 A0A010RP82 A0A015J5S5 A0A015JJV7 A0A015LKA2 A0A015M176 A0A016TC03 A0A016W7S1 A0A016W8M6 A0A017S851
(5648 more...)
Pyruvate dehydrogenase (acetyl-transferring). [EC: 1.2.4.1]
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
  • It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
5 A0A068XFH5 A0A0R3SY73 A0A0R3T0G1 A0A0R3UGF3 A0A0R3WCA9
Thiol oxidase. [EC: 1.8.3.2]
2 R'C(R)SH + O(2) = R'C(R)S-S(R)CR' + H(2)O(2).
  • R may be =S or =O, or a variety of other groups.
  • The enzyme is not specific for R'.
5 A0A0B7JM62 A0A0G4KF97 A0A0G4LS68 A0A166ZZ25 A0A194V1K1
Transferred entry: 3.4.25.1. [EC: 3.4.99.46]
    1 Q9ZRY9
    Phosphopyruvate hydratase. [EC: 4.2.1.11]
    2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.
    • Also acts on 3-phospho-D-erythronate.
    1 A0A0L1HSD7
    Homoserine dehydrogenase. [EC: 1.1.1.3]
    L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H.
    • The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+).
    • The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.
    1 A0A0N0RS64