View in Gene3D

CATH Superfamily 3.40.640.10

Type I PLP-dependent aspartate aminotransferase-like (Major domain)

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:

"
Type I PLP-dependent aspartate aminotransferase-like (Major domain)
".

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.
« Back to all FunFams

FunFam 33: Aspartate aminotransferase

There are 6 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
Methionine transaminase. [EC: 2.6.1.88]
L-methionine + a 2-oxo acid = 2-oxo-4-methylthiobutanoate + an L-amino acid.
  • The enzyme is most active with L-methionine.
  • It participates in the L-methionine salvage pathway from S-methyl- 5'-thioadenosine, a by-product of polyamine biosynthesis.
  • The enzyme from the bacterium Klebsiella pneumoniae can use several different amino acids as amino donor, with aromatic amino acids being the most effective.
  • The enzyme from the plant Arabidopsis thaliana is also a part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates.
 306 A0A070SRM4 A0A070SRM4 A0A070SRM4 A0A070SRM4 A0A070SRM4 A0A070SRM4 A0A070SRM4 A0A070SRM4 A0A070SRM4 A0A070SRM4
(296 more...)
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.
 49 A0A0C7D6N1 A0A0C7D6N1 A0A0C7D6N1 A0A0C7D6N1 A0A0C7D6N1 A0A0C7D6N1 A0A0C7D6N1 A0A1F0I790 A0A1F0I790 A0A1F0I790
(39 more...)
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