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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 31: Oxygen-dependent choline dehydrogenase

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
Choline dehydrogenase. [EC: 1.1.99.1]
Choline + acceptor = betaine aldehyde + reduced acceptor.
  • In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyze the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine.
  • In plants, the first reaction is catalyzed by EC 1.14.15.7 whereas in animals and many bacteria, it is catalyzed by either EC 1.1.99.1 or EC 1.1.3.17.
  • The enzyme involved in the second step, EC 1.2.1.8, appears to be the same in plants, animals and bacteria.
 1489 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8
(1479 more...)
Betaine-aldehyde dehydrogenase. [EC: 1.2.1.8]
Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH.
  • In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine.
  • This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria.
  • In contrast, different enzymes are involved in the first reaction.
  • In plants, this reaction is catalyzed by EC 1.14.15.7, whereas in animals and many bacteria, it is catalyzed by either membrane-bound EC 1.1.99.1 or soluble EC 1.1.3.17.
  • In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 and EC 2.1.1.157.
 1486 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8 A0A070SZD8
(1476 more...)
Glucose 1-dehydrogenase (FAD, quinone). [EC: 1.1.5.9]
D-glucose + a quinone = D-glucono-1,5-lactone + a quinol.
  • 2,6-dichloroindophenol can act as acceptor.
  • Cf. EC 1.1.5.2.
  • Formerly EC 1.1.99.10.
 2 P18172 P18173
5'-oxoaverantin cyclase. [EC: 4.2.1.142]
5'-oxoaverantin = (1'S,5'S)-averufin + H(2)O.
  • Isolated from the aflatoxin-producing mold Aspergillus parasiticus.
  • The enzyme also catalyzes the conversion of versiconal to versicolorin B (EC 4.2.1.143).
  • Involved in aflatoxin biosynthesis.
 1 Q12062
Versicolorin B synthase. [EC: 4.2.1.143]
Versiconal = versicolorin B + H(2)O.
  • Isolated from the aflatoxin-producing mold Aspergillus parasiticus.
  • Involved in aflatoxin biosynthesis.
 1 Q12062
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