View in Gene3D

CATH Superfamily 3.30.390.30

FAD/NAD-linked reductase, C-terminal dimerisation 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: 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.
« Back to all FunFams

FunFam 2529: Flavoprotein disulfide reductase

There are 2 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
NAD(P)H dehydrogenase (quinone). [EC: 1.6.5.2]
NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone.
  • The enzyme catalyzes a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone.
  • The animal, but not the plant, form of the enzyme is inhibited by dicoumarol.
  • Formerly EC 1.6.99.2.
 38 A0A045JT65 A0A0E8U4I6 A0A0H3MEF7 A0A0H3P5U3 A0A0T7LZP3 A0A0T9AV07 A0A0T9B680 A0A0T9CRP4 A0A0T9NVD8 A0A0T9VER4
(28 more...)
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.
 5 A0A0H3LFH3 A0A0H3MEF7 A0A0H3P5U3 A0A1A9EC39 A0A1K2NBS2