The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Aspartate Aminotransferase, domain 1
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 62: Aspartate aminotransferase A

There are 4 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Aspartate transaminase. [EC: 2.6.1.1]
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 E9L7A5 Q9SIE1
Glutamate--prephenate aminotransferase. [EC: 2.6.1.79]
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.
2 E9L7A5 Q9SIE1
Aspartate--prephenate aminotransferase. [EC: 2.6.1.78]
L-arogenate + oxaloacetate = prephenate + L-aspartate.
  • Glutamate can also act as the amino donor, but more slowly (cf. EC 2.6.1.79).
2 E9L7A5 Q9SIE1
Asparagine--oxo-acid transaminase. [EC: 2.6.1.14]
L-asparagine + a 2-oxo acid = 2-oxosuccinamate + an amino acid.
    1 Q8DTM1
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