CATH Classification

Domain Context

CATH Clusters

Superfamily Tetratricopeptide repeat domain
Functional Family UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Enzyme Information

2.4.1.255
Protein O-GlcNAc transferase.
based on mapping to UniProt O15294
(1) UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine. (2) UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine.
-!- 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 2.4.1.255 transfers GlcNAc onto substrate proteins and EC 3.2.1.169 cleaves GlcNAc from the modified proteins.

UniProtKB Entries (1)

O15294
OGT1_HUMAN
Homo sapiens
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

PDB Structure

PDB 4XIF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
Pathak, S., Alonso, J., Schimpl, M., Rafie, K., Blair, D.E., Borodkin, V.S., Schuttelkopf, A.W., Albarbarawi, O., van Aalten, D.M.
Nat.Struct.Mol.Biol.