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CATH Superfamily 3.40.30.10

Glutaredoxin

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:

"
Glutaredoxin
".

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 80170: Glutathione S-transferase domain protein

There are 5 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
Glutathione transferase. [EC: 2.5.1.18]
RX + glutathione = HX + R-S-glutathione.
  • A group of enzymes of broad specificity.
  • R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group.
  • Also catalyzes the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange.
  • Formerly EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and EC 4.4.1.7.
 768 A0A017HV88 A0A017HV88 A0A022PI80 A0A022PI80 A0A024K8M6 A0A024K8M6 A0A031GMI5 A0A031GMI5 A0A031GUM9 A0A031GUM9
(758 more...)
Glutathione peroxidase. [EC: 1.11.1.9]
2 glutathione + H(2)O(2) = glutathione disulfide + 2 H(2)O.
  • Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 on phospholipids, can act as acceptor, but more slowly than H(2)O(2) (cf. EC 1.11.1.12).
 2 A0A0L1HQ54 A0A0L1HQ54
Maleylacetoacetate isomerase. [EC: 5.2.1.2]
4-maleylacetoacetate = 4-fumarylacetoacetate.
  • Also acts on maleylpyruvate.
 2 D0IIY3 D0IIY3
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    		 2 A0A085U4X9 A0A085U4X9
    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 G8PWF4 G8PWF4
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