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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 41231: Aspartate transaminase

There are 1 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
Arginine--pyruvate transaminase. [EC: 2.6.1.84]
L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-alanine.
  • While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly.
  • Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor.
  • This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa.
  • This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked.
 6 A0A0C7D6N1 A0A0H3QVJ9 A0A0P1DHI5 A0A1E9C7J2 A0A1F0I790 Q9HUI9