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CATH Superfamily 3.50.50.60

FAD/NAD(P)-binding domain

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:

"
FAD/NAD(P)-binding domain
".

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 112428: Thioredoxin and glutathione reductase

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
Thioredoxin-disulfide reductase. [EC: 1.8.1.9]
Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH.
  • May be identical to EC 1.8.1.10.
  • Formerly EC 1.6.4.5.
 66 A0A023B5W7 A0A024W7T5 A0A060RSQ2 A0A074STX3 A0A077L6Y7 A0A0J9RZU9 A0A0J9TEX4 A0A0L7K885 A0A0L7M7V3 A0A0Q9W6K5
(56 more...)
Glutathione-disulfide reductase. [EC: 1.8.1.7]
2 glutathione + NADP(+) = glutathione disulfide + NADPH.
  • Activity is dependent on a redox-active disulfide in each of the active centers.
  • Formerly EC 1.6.4.2.
 46 A0A017H8A0 A0A074STX3 A0A086K8G2 A0A086KJU8 A0A086LBE1 A0A086LGG5 A0A086LME5 A0A086M6N7 A0A086PQ35 A0A086QKA0
(36 more...)
Transferred entry: 1.8.1.7. [EC: 1.6.4.2]
    		3 P91884 Q9FSG8 Q9M3T6
    Transferred entry: 1.8.1.9. [EC: 1.6.4.5]
      		2 Q8MZM6 Q962Y6
      Dihydrolipoyl dehydrogenase. [EC: 1.8.1.4]
      Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.
      • A component of the multienzyme 2-oxo-acid dehydrogenase complexes.
      • In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups.
      • It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes.
      • Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine.
      • It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate.
      • Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase.
      • The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein.
      • Formerly EC 1.6.4.3.
      		 1 A0A0W4ZHD1