CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| Functional Family | Serine hydroxymethyltransferase |
Enzyme Information
| 2.1.2.- |
Hydroxymethyl-, formyl- and related transferases.
based on mapping to UniProt Q58992
|
| 4.1.2.49 |
L-allo-threonine aldolase.
based on mapping to UniProt Q58992
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)
| Q58992 |
GLYA_METJA
Methanocaldococcus jannaschii DSM 2661
Serine hydroxymethyltransferase
|
PDB Structure
| PDB | 4BHD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Crystal Structure of Archaeal Serine Hydroxymethyltransferase Reveals Idiosyncratic Features Likely Required to Withstand High Temperatures.
Proteins
|
