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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 79966: Threonine aldolase, low-specificity

There are 2 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
L-threonine aldolase. [EC: 4.1.2.5]
L-threonine = glycine + acetaldehyde.
  • This enzyme is specific for L-threonine and can not utilize L-allo- threonine.
  • Different from EC 4.1.2.49 and EC 4.1.2.48.
 13 A0A0F7A396 A0A0N0WJW8 A0A0N1JA54 A0A0N8QK09 A0A0P9RI46 A0A0P9WEW3 A0A0Q0BEI8 A0A132FEM3 A0A1E3XYA7 F3K5F6
(3 more...)
Low-specificity L-threonine aldolase. [EC: 4.1.2.48]
(1) L-threonine = glycine + acetaldehyde. (2) L-allo-threonine = glycine + acetaldehyde.
  • The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine.
  • The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine.
  • The enzyme can also catalyze the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis.
  • Different from EC 4.1.2.5 and EC 4.1.2.49.
 1 A0A193SPN5