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 | Aspartate aminotransferase A |
Enzyme Information
| 2.6.1.1 |
Aspartate transaminase.
based on mapping to UniProt Q9SIE1
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
-!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. -!- This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
|
| 2.6.1.78 |
Aspartate--prephenate aminotransferase.
based on mapping to UniProt Q9SIE1
L-arogenate + oxaloacetate = prephenate + L-aspartate.
-!- Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79).
|
| 2.6.1.79 |
Glutamate--prephenate aminotransferase.
based on mapping to UniProt Q9SIE1
L-arogenate + 2-oxoglutarate = prephenate + L-glutamate.
-!- Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78). -!- The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate.
|
UniProtKB Entries (1)
| Q9SIE1 |
PAT_ARATH
Arabidopsis thaliana
Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
|
PDB Structure
| PDB | 5WML |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis.
Plant J.
|