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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 196: L-amino acid oxidase LaoA

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
L-amino-acid oxidase. [EC: 1.4.3.2]
An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
    		 4 A0A0B0E7H0 A0A0B0E7H0 P23623 P23623
    7-chloro-L-tryptophan oxidase. [EC: 1.4.3.23]
    7-chloro-L-tryptophan + O(2) = 2-imino-3-(7-chloroindol-3-yl)propanoate + H(2)O(2).
    • This enzyme catalyzes a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes.
    • During catalysis, the bound FAD is reoxidized at the expense of molecular oxygen, producing one molecule of hydrogen peroxide.
    • The enzyme shows significant preference for 7-chloro-L-tryptophan over L-tryptophan.
    		 1 Q8KHS0
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