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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 15596: Glutathione S-transferase, N-terminal domain

There are 6 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.
 901 A0A009G6K7 A0A009HS95 A0A009HTG3 A0A009JQC0 A0A009QHZ7 A0A009RBH3 A0A009SJC0 A0A011SJ39 A0A017H9K7 A0A017HBC7
(891 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).
 13 A0A0E2CX45 A0A0L1HQ54 A0A0L8VI99 A0A109I4C5 A6ZRL3 B3LP70 B5VQI2 C8ZG05 E7KHF2 E7QJN9
(3 more...)
Maleylacetoacetate isomerase. [EC: 5.2.1.2]
4-maleylacetoacetate = 4-fumarylacetoacetate.
  • Also acts on maleylpyruvate.
 2 D0IIY3 E0SKK1
DDT-dehydrochlorinase. [EC: 4.5.1.1]
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2- bis(4-chlorophenyl)ethylene + chloride.
    		 2 A0A0E2CX45 A0A109I4C5
    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.
    		 1 G8PWF4
    Peroxidase. [EC: 1.11.1.7]
    2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
      		 1 A0A085U4X9
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