CATH Classification

Domain Context

CATH Clusters

Superfamily Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Functional Family

Enzyme Information

3.4.25.1
Proteasome endopeptidase complex.
based on mapping to UniProt P9WHT9
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.

UniProtKB Entries (1)

P9WHU1
PSA_MYCTU
Mycobacterium tuberculosis H37Rv
Proteasome subunit alpha

PDB Structure

PDB 3MI0
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome.
Li, D., Li, H., Wang, T., Pan, H., Lin, G., Li, H.
Embo J.