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CATH Superfamily 3.30.390.50

CO dehydrogenase flavoprotein, C-terminal 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:

"
CO dehydrogenase flavoprotein, C-terminal 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 3: Aldehyde oxidase1

There are 4 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
Indole-3-acetaldehyde oxidase. [EC: 1.2.3.7]
(Indol-3-yl)acetaldehyde + H(2)O + O(2) = (indol-3-yl)acetate + H(2)O(2).
  • Isoform of EC 1.2.3.1.
  • Has a preference for aldehydes having an indole-ring structure as substrate.
  • May play a role in plant hormone biosynthesis as its activity is higher in the auxin-overproducing mutant, super-root1, than in wild- type Arabidopsis thaliana.
  • While (indol-3-yl)acetaldehyde is the preferred substrate, it also oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly.
 9 A0A178WM01 A0A178WM01 O23887 O23888 Q7G191 Q7G191 Q7G192 Q7G193 Q7G9P4
Aldehyde oxidase. [EC: 1.2.3.1]
An aldehyde + H(2)O + O(2) = a carboxylate + H(2)O(2).
  • The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides.
  • The enzyme is also responsible for the oxidation of retinal, an activity that was initially attributed to a distinct enzyme (EC 1.2.3.11).
  • Formerly EC 1.2.3.11.
 4 A0A178WM01 A0A178WM01 Q7G191 Q7G191
Abscisic-aldehyde oxidase. [EC: 1.2.3.14]
Abscisic aldehyde + H(2)O + O(2) = abscisate + H(2)O(2).
  • Acts on both (+)- and (-)-abscisic aldehyde.
  • Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.1.1.288, EC 1.13.11.51 and EC 1.14.13.93.
  • While abscisic aldehyde is the best substrate, the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and benzaldehyde as substrates, but more slowly.
 1 Q7G9P4
Xanthine dehydrogenase. [EC: 1.17.1.4]
Xanthine + NAD(+) + H(2)O = urate + NADH.
  • Acts on a variety of purines and aldehydes, including hypoxanthine.
  • The mammalian enzyme can also convert all-trans retinol to all-trans- retinoate, while the substrate is bound to a retinoid-binding protein.
  • The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum center.
  • The mammallian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4).
  • During purification the enzyme is largely converted to an O(2)- dependent form, EC 1.17.3.2.
  • The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion.
  • The conversion can also occur in vivo.
  • Formerly EC 1.2.1.37 and EC 1.1.1.204.
 1 R4ZGN4
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