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CATH Superfamily 3.90.1150.10

Aspartate Aminotransferase, domain 1

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_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 80417: Bifunctional phosphonoacetaldehyde hydrolase/amino...

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
2-aminoethylphosphonate--pyruvate transaminase. [EC: 2.6.1.37]
(2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine.
  • 2-aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.
 3510 A0A009GSF7 A0A009GSF7 A0A009H8A8 A0A009H8A8 A0A009IQS9 A0A009IQS9 A0A009JQV5 A0A009JQV5 A0A009N2J0 A0A009N2J0
(3500 more...)
Phosphonoacetaldehyde hydrolase. [EC: 3.11.1.1]
Phosphonoacetaldehyde + H(2)O = acetaldehyde + phosphate.
  • This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken.
  • The mechanism is similar to that used by EC 4.1.2.13 to break a C-C bond.
 16 A0A069AED3 A0A069AED3 Q183T0 Q183T0 T3DAC3 T3DAC3 T4H8K7 T4H8K7 U3UGG7 U3UGG7
(6 more...)
Alanine--glyoxylate transaminase. [EC: 2.6.1.44]
L-alanine + glyoxylate = pyruvate + glycine.
  • With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate.
  • A second component also catalyzes the reaction of EC 2.6.1.51.
 10 A0A0B7AUC3 A0A0B7AUC3 A7SHM7 A7SHM7 C3Y0B7 C3Y0B7 K1QDM9 K1QDM9 T1JE68 T1JE68
Serine--pyruvate transaminase. [EC: 2.6.1.51]
L-serine + pyruvate = 3-hydroxypyruvate + L-alanine.
  • The liver enzyme may be identical with EC 2.6.1.44.
 10 A0A0B7AUC3 A0A0B7AUC3 A7SHM7 A7SHM7 C3Y0B7 C3Y0B7 K1QDM9 K1QDM9 T1JE68 T1JE68
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