CATH Domain 5wmhE01

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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)

PAT_ARATH

Arabidopsis thaliana

Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase

PDB Structure

PDB	5WMH
External Links	PDBSum Proteopedia
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.