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CATH Superfamily 3.30.43.10

Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, 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 12066: Xanthine dehydrogenase, A 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]
(1) Xanthine + NAD(+) + H(2)O = urate + NADH. (2) Hypoxanthine + NAD(+) + H(2)O = xanthine + 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.
 33 A0A031IVF0 A0A061D2R8 A0A086BXJ0 A0A098FKD6 A0A0E3K8X6 A0A0F4XNH5 A0A0H2Z8N3 A0A0P8X9L3 A0A0V2NUM8 A0A157WNF1
(23 more...)
4-hydroxybenzoyl-CoA reductase. [EC: 1.3.7.9]
Benzoyl-CoA + oxidized ferredoxin = 4-hydroxybenzoyl-CoA + reduced ferredoxin.
  • Involved in the anaerobic pathway of phenol metabolism in bacteria.
  • A ferredoxin with two [4Fe-4S] clusters functions as the natural electron donor.
  • Formerly EC 1.3.99.20.
 20 A0A069Q2H3 A0A0B7D5X8 A0A0D0SNX3 A0A0H2Z8N3 A0A0P1DDP2 A0A0Q8YWR0 A0A0R3C987 A0A0S4HPX7 A0A0U3T205 A0A0V8T441
(10 more...)
Xanthine oxidase. [EC: 1.17.3.2]
Xanthine + H(2)O + O(2) = urate + H(2)O(2).
  • Also oxidizes hypoxanthine, some other purines and pterins, and aldehydes, but is distinct from EC 1.2.3.1.
  • Under some conditions the product is mainly superoxide rather than peroxide: R-H + H(2)O + 2 O(2) = ROH + 2 O(2)(.-) + 2 H(+).
  • The mammallian enzyme predominantly exists as an NAD-dependent dehydrogenase (EC 1.17.1.4).
  • During purification the enzyme is largely converted to the O(2)- dependent xanthine oxidase 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 1.1.3.22 and EC 1.2.3.2.
 4 A0A0F4XNH5 G8Q001 W6VIP8 W6VS29
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