×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Hyaluronidase post-catalytic domain-like
Functional Family

Enzyme Information

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 (1)

Q0TR53
OGA_CLOP1
Clostridium perfringens ATCC 13124
O-GlcNAcase NagJ

PDB Structure

PDB 2CBI
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis.
Rao, F.V., Dorfmueller, H.C., Villa, F., Allwood, M., Eggleston, I.M., van Aalten, D.M.
EMBO J.
CATH-Gene3D is a Global Biodata Core Resource Learn more...