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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 4: Xanthine dehydrogenase, FAD binding subunit

There are 3 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
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.
 3297 A0A026UVK0 A0A026UVK0 A0A026UVK0 A0A026UVK0 A0A026UVK0 A0A026UVK0 A0A026UVK0 A0A026UVK0 A0A026UVK0 A0A026UVK0
(3287 more...)
Aerobic carbon monoxide dehydrogenase. [EC: 1.2.5.3]
CO + a quinone + H(2)O = CO(2) + a quinol.
  • This enzyme, found in carboxydotrophic bacteria, catalyzes the oxidation of CO to CO(2) under aerobic conditions.
  • The enzyme belongs to the xanthine oxidoreductase family.
  • The CO(2) that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor.
  • Cf. EC 1.2.7.4.
 1 P19914
Caffeine dehydrogenase. [EC: 1.17.5.2]
Caffeine + ubiquinone + H(2)O = 1,3,7-trimethylurate + ubiquinol.
  • This enzyme, characterized from the soil bacterium Pseudomonas sp. CBB1, catalyzes the incorporation of an oxygen atom originating from a water molecule into position C-8 of caffeine.
  • The enzyme utilizes short-tail ubiquinones as the preferred electron acceptor.
 1 D7REY4
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