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CATH Superfamily 3.30.9.10

D-Amino Acid Oxidase, subunit A, domain 2

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:

"
D-Amino Acid Oxidase, subunit A, domain 2
".

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 264: FAD-dependent catabolic D-arginine dehydrogenase D...

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
D-arginine dehydrogenase. [EC: 1.4.99.6]
D-arginine + acceptor + H(2)O = 5-guanidino-2-oxopentanoate + NH(3) + reduced acceptor.
  • The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25 a two-enzyme complex involved in the racemization of D- and L-arginine.
  • The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate.
  • However, activity is maximal with D-arginine and D-lysine.
  • Not active on glycine.
  • Formerly EC 1.4.99.1.
 2 A0A454LT47 Q9HXE3
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