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 | Low-specificity L-threonine aldolase |
Enzyme Information
| 4.1.2.49 |
L-allo-threonine aldolase.
based on mapping to UniProt O07051
L-allo-threonine = glycine + acetaldehyde.
-!- This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine. -!- Different from EC 4.1.2.5 and EC 4.1.2.48. -!- A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1.
|
UniProtKB Entries (1)
| O07051 |
LTAA_AERJA
Aeromonas jandaei
L-allo-threonine aldolase
|
PDB Structure
| PDB | 3WGC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
L-allo-Threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.
Acta Crystallogr.,Sect.D
|
