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 7695: Dihydrolipoyl dehydrogenase

There are 3 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
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.
 1379 A0A010QEH1 A0A011LX85 A0A014MCK1 A0A017IQ44 A0A022PNJ2 A0A023E8H4 A0A023RFG0 A0A023V904 A0A023YRY1 A0A024KL43
(1369 more...)
Adenine phosphoribosyltransferase. [EC: 2.4.2.7]
AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate.
  • 5-amino-4-imidazolecarboxamide can replace adenine.
 1 A4N3Z7
Dihydrolipoyllysine-residue acetyltransferase. [EC: 2.3.1.12]
Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-acetyldihydrolipoyl)lysine.
  • A multimer (24-mer or 60-mer, depending on the source) of this enzyme forms the core of the pyruvate dehydrogenase multienzyme complex, and binds tightly both EC 1.2.4.1 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively acetylated by EC 1.2.4.1, and the only observed direction catalyzed by EC 2.3.1.12 is that where the acetyl group is passed to coenzyme A.
 1 K8BTS7