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 | Phosphoserine aminotransferase |
Enzyme Information
| 2.6.1.52 |
Phosphoserine transaminase.
based on mapping to UniProt P23721
(1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + L-glutamate.
-!- Catalyzes the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli. -!- Also catalyzes the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in E.coli (using reaction 2 above). -!- In E.coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). -!- Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis. -!- Non-phosphorylated forms of serine and threonine are not substrates.
|
UniProtKB Entries (1)
| P23721 |
SERC_ECOLI
Escherichia coli K-12
Phosphoserine aminotransferase
|
PDB Structure
| PDB | 1BJN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate.
J.Mol.Biol.
|
