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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 112385: Dimethylaniline monooxygenase [N-oxide-forming] 4

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
Flavin-containing monooxygenase. [EC: 1.14.13.8]
N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + NADP(+) + H(2)O.
  • A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines.
  • Is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate.
  • Generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites.
  • For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl- 1,2,3,6-tetrahydropyridine (MPTP).
  • Formerly EC 1.13.12.11.
 54 A0A023JCA1 A0A023JCQ5 A0A024R8Z4 A0A091CYA5 A0A0B8RUR8 A0A0D9RGQ9 A0A0D9S0K5 A0A0G2JSI0 A0A131XI95 A8KB08
(44 more...)
Trimethylamine monooxygenase. [EC: 1.14.13.148]
N,N,N-trimethylamine + NADPH + O(2) = N,N,N-trimethylamine N-oxide + NADP(+) + H(2)O.
  • The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy.
  • The mammalian enzyme is involved in detoxification of trimethylamine.
  • Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome).
 6 A0A024R8Z4 P31513 Q7YS44 Q8HYJ9 Q8SPQ7 Q95LA1