CATH Domain 4xi9C02

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.25	Alpha Horseshoe
	1.25.40	Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
	1.25.40.10	Tetratricopeptide repeat domain

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	4XI9
External Links	PDBSum Proteopedia
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.