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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_2_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 17127: Xanthine dehydrogenase FAD-binding subunit

There are 16 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
Transferred entry: 1.2.7.4. [EC: 1.2.99.2]
    		896 A0A021X303 A0A021X303 A0A031HNV8 A0A031HNV8 A0A045INY7 A0A045INY7 A0A059MR94 A0A059MR94 A0A060IBV3 A0A060IBV3
    (886 more...)
    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.
    		 244 A0A034T350 A0A034T350 A0A073D3Q2 A0A073D3Q2 A0A075KCC9 A0A075KCC9 A0A076LQE2 A0A076LQE2 A0A081KGW0 A0A081KGW0
    (234 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.
    		 172 A0A0F0CFL9 A0A0F0CFL9 A0A0F0CHZ1 A0A0F0CHZ1 A0A0H3IY13 A0A0H3IY13 A0A0J1F8S5 A0A0J1F8S5 A0A0J1FB96 A0A0J1FB96
    (162 more...)
    6-hydroxypseudooxynicotine dehydrogenase. [EC: 1.5.99.14]
    1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + acceptor + H(2)O = 1-(2,6-dihydroxypyridin-3-yl)-4-(methylamino)butan-1-one + reduced acceptor.
    • Contains a cytidylyl molybdenum cofactor.
    • The enzyme, which participates in the nicotine degradation pathway, has been characterized from the soil bacterium Arthrobacter nicotinovorans.
    		 66 A0A066PMM7 A0A066PMM7 A0A0J1FK98 A0A0J1FK98 A0A0J6WMK8 A0A0J6WMK8 A0A0J6Y4A6 A0A0J6Y4A6 A0A0K0Y2K6 A0A0K0Y2K6
    (56 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.
    		 16 A0A157QTC9 A0A157QTC9 A0A157SBZ5 A0A157SBZ5 A0A163Z1R9 A0A163Z1R9 A0A168K4F5 A0A168K4F5 A0A1B8P2R1 A0A1B8P2R1
    (6 more...)
    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.
    		 16 A0A0S3PZS6 A0A0S3PZS6 A0A0S3Q043 A0A0S3Q043 A0A0U5LT78 A0A0U5LT78 A0A177HUF2 A0A177HUF2 A0A178WZR4 A0A178WZR4
    (6 more...)
    Transferred entry: 1.3.7.9. [EC: 1.3.99.20]
      		10 B3R8T3 B3R8T3 K0NF27 K0NF27 K0NQ86 K0NQ86 Q0K383 Q0K383 R7XID1 R7XID1
      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.
      		 10 A0A0U3GXB0 A0A0U3GXB0 A0A151ABN8 A0A151ABN8 M1I8F8 M1I8F8 M1JFQ1 M1JFQ1 Q4J6M6 Q4J6M6
      Nicotine dehydrogenase. [EC: 1.5.99.4]
      Nicotine + acceptor + H(2)O = (S)-6-hydroxynicotine + reduced acceptor.
      • Acts on both (R)- and (S)-isomers.
      		 8 A0A0C9T2E2 A0A0C9T2E2 A0A1D9FF74 A0A1D9FF74 C1B578 C1B578 Q59127 Q59127
      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.
      		 4 P19914 P19914 P19920 P19920
      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 A0A0D5M2C4 A0A0D5M2C4 F6CX84 F6CX84
      Nitrite reductase (NAD(P)H). [EC: 1.7.1.4]
      Ammonia + 3 NAD(P)(+) + 2 H(2)O = nitrite + 3 NAD(P)H.
      • The enzymes from the fungi Neurospora crassa, Emericella nidulans and Candida nitratophila and the bacterium Aliivibrio fischeri can use either NADPH or NADH as electron donor.
      • Cf. EC 1.7.1.15.
      • Formerly EC 1.6.6.4.
      		 2 C0QAS4 C0QAS4
      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.
      		 2 A0A1B7IBJ0 A0A1B7IBJ0
      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.
      		 2 F9VNL6 F9VNL6
      Transferred entry: 1.17.1.4. [EC: 1.1.1.204]
        		2 Q1Q1A2 Q1Q1A2
        Indolepyruvate decarboxylase. [EC: 4.1.1.74]
        3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO(2).
        • More specific than EC 4.1.1.1.
        		 2 F9VNL6 F9VNL6
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