CATH Classification

Domain Context

CATH Clusters

Superfamily Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Functional Family UDP-N-acetylhexosamine pyrophosphorylase isoform X2

Enzyme Information
UDP-N-acetylglucosamine diphosphorylase.
based on mapping to UniProt Q16222
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine.
-!- Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. -!- The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC -!- The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC, while the bacterial enzyme shows low activity toward that substrate.
UDP-N-acetylgalactosamine diphosphorylase.
based on mapping to UniProt Q16222
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-galactosamine.
-!- The enzyme from plants and animals also has activity toward N-acetyl- alpha-D-glucosamine 1-phosphate (cf. EC

UniProtKB Entries (1)

Homo sapiens
UDP-N-acetylhexosamine pyrophosphorylase

PDB Structure

External Links
Organism Escherichia
Primary Citation
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.
Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F., Bourne, Y.