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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 138: Flavin-containing monooxygenase

There are 1 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
Senecionine N-oxygenase. [EC: 1.14.13.101]
Senecionine + NADPH + O(2) = senecionine N-oxide + NADP(+) + H(2)O.
  • NADH cannot replace NADPH.
  • While pyrrolizidine alkaloids of the senecionine and monocrotaline types are generally good substrates (e.g. senecionine, retrorsine and monocrotaline), the enzyme does not use ester alkaloids lacking an hydroxy group at C-7 (e.g. supinine and phalaenopsine), 1,2-dihydro- alkaloids (e.g. sarracine) or unesterified necine bases (e.g. senkirkine) as substrates.
  • Senecionine N-oxide is used by insects as a chemical defense: it is non-toxic, but it is bioactivated to a toxic form by the action of cytochrome P450 oxidase when absorbed by insectivores.
 1 Q8MP06