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CATH Superfamily 3.30.470.10

Aminotransferase class 4, branched-chain amino acid transferase, N-terminal 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: waiting to be named.

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 3: Branched-chain-amino-acid aminotransferase

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
Branched-chain-amino-acid transaminase. [EC: 2.6.1.42]
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
  • Also acts on L-isoleucine and L-valine.
  • Different from EC 2.6.1.66.
 22 A0A178WB05 A0A178WB05 A0A384KYR5 A0A384KYR5 A0A384KYR5 B9DFH1 B9DFH1 B9DHH5 B9DHH5 Q0WQT2
(12 more...)
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.
 2 Q9LE06 Q9M401
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