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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_3_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 26: Succinate dehydrogenase flavoprotein subunit

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
L-aspartate oxidase. [EC: 1.4.3.16]
L-aspartate + O(2) = iminosuccinate + H(2)O(2).
  • L-aspartate oxidase catalyzes the first step in the de novo biosynthesis of NAD(+) in some bacteria.
  • O(2) can be replaced by fumarate as electron acceptor, yielding succinate.
  • The ability of the enzyme to use both O(2) and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions.
  • Iminosuccinate can either be hydrolyzed to form oxaloacetate and NH(3) or can be used by EC 2.5.1.72 in the production of quinolinate.
 66 A0A0H3M4A0 A0A0H3M4A0 A0A0H3M4A0 A0A0H3M4A0 A0A0H3M4A0 A0A0H3M4A0 A0A162S3M3 A0A162S3M3 A0A162S3M3 A0A162S3M3
(56 more...)
Succinate dehydrogenase (quinone). [EC: 1.3.5.1]
Succinate + a quinone = fumarate + a quinol.
  • The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria.
  • It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II).
  • In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone.
  • Cf. EC 1.3.5.4.
 1 Q0QF17
Fumarate reductase (CoM/CoB). [EC: 1.3.4.1]
Fumarate + CoM + CoB = succinate + CoM-S-S-CoB.
  • The enzyme, isolated from the archaeon Methanobacterium thermoautotrophicum, is very oxygen sensitive.
  • It cannot use reduced flavins, reduced coenzyme F420, or NAD(P)H as an electron donor.
  • Distinct from EC 1.3.1.6, EC 1.3.5.1 and EC 1.3.5.4.
  • Formerly EC 1.3.98.2.
 1 D9PU00
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