CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
Domain Context
CATH Clusters
| Superfamily | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
| Functional Family | UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase |
Enzyme Information
| 2.6.1.92 |
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase.
based on mapping to UniProt O25130
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate.
-!- The enzyme transfers the primary amino group of L-glutamate to C-4'' of UDP-4-dehydro sugars, forming a C-N bond in a stereo configuration opposite to that of UDP. -!- The enzyme from the bacterium Bacillus cereus has been shown to act on UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose, UDP-beta- L-threo-pentapyranos-4-ulose, UDP-4-dehydro-6-deoxy-D-glucose, and UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose. -!- Cf. EC 2.6.1.34, which catalyzes a similar reaction, but forms the C-N bond in the same stereo configuration as that of UDP.
|
UniProtKB Entries (1)
| O25130 |
PSEC_HELPY
Helicobacter pylori 26695
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase
|
PDB Structure
| PDB | 2FNU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural and Functional Characterization of PseC, an Aminotransferase Involved in the Biosynthesis of Pseudaminic Acid, an Essential Flagellar Modification in Helicobacter pylori
J.Biol.Chem.
|
