CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.420 | Nucleotidyltransferase; domain 5 |
|
3.30.420.40 | ATPase, nucleotide binding domain |
Domain Context
CATH Clusters
| Superfamily | 3.30.420.40 |
| Functional Family | Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase |
Enzyme Information
| 3.2.1.183 |
UDP-N-acetylglucosamine 2-epimerase (hydrolyzing).
based on mapping to UniProt Q9Y223
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.
|
| 2.7.1.60 |
N-acylmannosamine kinase.
based on mapping to UniProt Q9Y223
ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate.
-!- Acts on the acetyl and glycolyl derivatives.
|
UniProtKB Entries (1)
| Q9Y223 |
GLCNE_HUMAN
Homo sapiens
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
|
PDB Structure
| PDB | 2YHY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structures of N-Acetylmannosamine Kinase Provide Insights Into Enzyme Specificity and Inhibition
J.Biol.Chem.
|
