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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 81466: Alanine aminotransferase 2, mitochondrial

There are 7 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 transaminase. [EC: 2.6.1.2]
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.
  • 2-aminobutanoate acts slowly instead of alanine.
 1620 A0A014NMM5 A0A014NMM5 A0A017IEE2 A0A017IEE2 A0A022PHT1 A0A022PHT1 A0A023EBD7 A0A023EBD7 A0A023VE18 A0A023VE18
(1610 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.
 1032 A0A023VE18 A0A023VE18 A0A023Z059 A0A023Z059 A0A024KY41 A0A024KY41 A0A025CEC6 A0A025CEC6 A0A026RVR5 A0A026RVR5
(1022 more...)
Valine--pyruvate transaminase. [EC: 2.6.1.66]
L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine.
  • Different from EC 2.6.1.42.
 28 A0A022PHT1 A0A022PHT1 A0A081S0B8 A0A081S0B8 A0A0A0CLQ1 A0A0A0CLQ1 A0A0F7LRQ2 A0A0F7LRQ2 A0A1B1NMW7 A0A1B1NMW7
(18 more...)
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.
 8 A0A178WFM8 A0A178WFM8 A0A178WG36 A0A178WG36 Q9LR30 Q9LR30 Q9S7E9 Q9S7E9
Glycine transaminase. [EC: 2.6.1.4]
Glycine + 2-oxoglutarate = glyoxylate + L-glutamate.
    		 8 A0A178WFM8 A0A178WFM8 A0A178WG36 A0A178WG36 Q9LR30 Q9LR30 Q9S7E9 Q9S7E9
    Alanine--oxo-acid transaminase. [EC: 2.6.1.12]
    L-alanine + a 2-oxo acid = pyruvate + an L-amino acid.
      		 2 A0A171B308 A0A171B308
      Lysine/arginine leucyltransferase. [EC: 2.3.2.6]
      (1) L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-lysyl-[protein]. (2) L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-arginyl-[protein].
      • Participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue.
      • Once modified, the proteins are recognized by EC 3.4.21.92.
      • The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo.
      • Cf. EC 2.3.2.8 and EC 2.3.2.29.
      		 2 A0A085U4W4 A0A085U4W4