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CATH Superfamily 1.20.1050.10

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: 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 15492: Glutathione S-transferase family 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.
 1000 A0A011QTK7 A0A011QTK7 A0A023Z2V4 A0A023Z2V4 A0A024H2B9 A0A024H2B9 A0A024K7G5 A0A024K7G5 A0A024KNB5 A0A024KNB5
(990 more...)
Glutathione dehydrogenase (ascorbate). [EC: 1.8.5.1]
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.
    		 22 A0A0L8VLX5 A0A0L8VLX5 A7A035 A7A035 B3LRF0 B3LRF0 C7GXD4 C7GXD4 C8ZCN7 C8ZCN7
    (12 more...)
    Transferred entry: 2.3.2.23, 2.3.2.27 and 6.2.1.45. [EC: 6.3.2.19]
      		4 F7PF29 F7PF29 U2FXN5 U2FXN5
      Fructose-bisphosphate aldolase. [EC: 4.1.2.13]
      D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
      • Also acts on (3S,4R)-ketose 1-phosphates.
      • The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
      • Formerly EC 4.1.2.7.
      		 4 A0A031FPY6 A0A031FPY6 G9A2Y9 G9A2Y9
      Peptidylprolyl isomerase. [EC: 5.2.1.8]
      Peptidylproline (omega=180) = peptidylproline (omega=0).
      • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
      • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
      • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
      		 2 G9N5L1 G9N5L1
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