CATH Classification

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.
Holland, C.K., Berkovich, D.A., Kohn, M.L., Maeda, H., Jez, J.M.
Plant J.