The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Glycogen Phosphorylase B;
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
« Back to all FunFams

FunFam 25471: UDP-N-acetylglucosamine 2-epimerase (Uridine dipho...

There are 3 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing). [EC: 5.1.3.14]
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine.
  • This bacterial enzyme catalyzes the reversible interconversion of UDP-GlcNAc and UDP-ManNAc.
  • The latter is used in a variety of bacterial polysaccharide biosyntheses.
  • Cf. EC 3.2.1.183.
9 A0A0E0TMJ5 A1KRA2 A8V8Z2 C6SME7 E3D5C1 H2VFI5 M5DAK1 Q57141 Q79DD9
N-acylmannosamine kinase. [EC: 2.7.1.60]
ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate.
  • Acts on the acetyl and glycolyl derivatives.
6 A0A0E0TMJ5 A1KRA2 C6SME7 H2VFI5 Q57141 Q79DD9
UDP-N-acetylglucosamine 2-epimerase (hydrolyzing). [EC: 3.2.1.183]
UDP-N-acetyl-alpha-D-glucosamine + H(2)O = N-acetyl-D-mannosamine + UDP.
  • The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus.
  • It catalyzes the first step of sialic acid (N-acetylneuraminic acid) biosynthesis.
  • The initial product formed is the alpha anomer, which rapidly mutarotates to a mixture of anomers.
  • The mammalian enzyme is bifunctional and also catalyzes EC 2.7.1.60.
  • Cf. EC 5.1.3.14.
6 A0A0E0TMJ5 A1KRA2 C6SME7 H2VFI5 Q57141 Q79DD9
CATH-Gene3D is a Global Biodata Core Resource Learn more...