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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 81469: Alanine--glyoxylate aminotransferase 2, mitochondr...

There are 3 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
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.
 6 B9T1D1 Q17QF0 Q3UEG6 Q5RFA3 Q64565 Q9BYV1
(R)-3-amino-2-methylpropionate--pyruvate transaminase. [EC: 2.6.1.40]
(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine.
  • The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.22, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
  • Formerly EC 2.6.1.61.
 5 Q17QF0 Q3UEG6 Q5RFA3 Q64565 Q9BYV1
Gamma-glutamyltransferase. [EC: 2.3.2.2]
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
  • The mammlian enzyme is part of the cell antioxidant defense mechanism.
  • It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels.
  • The protein also has EC 3.4.19.13 activity.
  • The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide.
  • The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions.
 1 A0A0B2RG74