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CATH Superfamily 3.30.465.10

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: waiting to be named.

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 17: Xanthine dehydrogenase, FAD binding subunit

There are 5 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...)
Glyceraldehyde dehydrogenase (FAD-containing). [EC: 1.2.99.8]
D-glyceraldehyde + H(2)O + acceptor = D-glycerate + reduced acceptor.
  • The enzyme from the archaeon Sulfolobus acidocaldarius catalyzes the oxidation of D-glyceraldehyde in the nonphosphorylative Entner- Doudoroff pathway.
  • With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde.
  • It is not known which acceptor is utilized in vivo.
 16 A0A0U3GXB0 A0A0U3GXB0 A0A0U3GXB0 A0A0U3GXB0 M1I8F8 M1I8F8 M1I8F8 M1I8F8 M1JFQ1 M1JFQ1
(6 more...)
Nicotinate dehydrogenase. [EC: 1.17.1.5]
Nicotinate + H(2)O + NADP(+) = 6-hydroxynicotinate + NADPH.
  • The enzyme is capable of acting on a variety of nicotinate analogs to varying degrees, including pyrazine-2-carboxylate, pyrazine 2,3- dicarboxylate, trigonelline and 6-methylnicotinate.
  • The enzyme from Clostridium barkeri also possesses a catalytically essential, labile selenium that can be removed by reaction with cyanide.
  • Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri.
  • Other enzymes involved in this pathway are EC 1.3.7.1, EC 3.5.2.18, EC 1.1.1.291, EC 5.4.99.4, EC 5.3.3.6, EC 4.2.1.85 and EC 4.1.3.32.
  • Formerly EC 1.5.1.13.
 4 A0A1H3FYA8 A0A1H3FYA8 Q0QLF4 Q0QLF4
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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