CATH Classification

Domain Context

CATH Clusters

Superfamily Chitobiase/beta-hexosaminidase domain 2-like
Functional Family

Enzyme Information

3.2.1.52
Beta-N-acetylhexosaminidase.
based on mapping to UniProt Q0TR53
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
-!- Acts on N-acetylglucosides and N-acetylgalactosides. -!- Formerly EC 3.2.1.29 and EC 3.2.1.30.
3.2.1.169
Protein O-GlcNAcase.
based on mapping to UniProt Q0TR53
(1) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine. (2) [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-glucosamine.
-!- Within higher eukaryotes post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. -!- EC 2.4.1.155 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.

UniProtKB Entries (2)

O60502
OGA_HUMAN
Homo sapiens
Protein O-GlcNAcase
Q0TR53
OGA_CLOP1
Clostridium perfringens ATCC 13124
O-GlcNAcase NagJ

PDB Structure

PDB 2YDQ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Synergy of Peptide and Sugar in O-Glcnacase Substrate Recognition.
Schimpl, M., Borodkin, V.S., Gray, L.J., Van Aalten, D.M.F.
Chem.Biol.