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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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 13 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
Lipoate--protein ligase. [EC: 6.3.1.20]
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine = a [lipoyl- carrier protein]-N(6)-(lipoyl)lysine + AMP + diphosphate.
  • This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid.
  • The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein).
  • Lipoylation is essential for the function of these enzymes.
  • The enzyme can also use octanoate instead of lipoate.
  • Formerly EC 2.7.7.63.
 255 A0A024L941 A0A026V5G3 A0A029IE97 A0A029J358 A0A066RDU8 A0A070SRA2 A0A070UZ28 A0A073FLC3 A0A090NZ37 A0A0A0F6X9
(245 more...)
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.
 81 A0A026UVK0 A0A028ADL4 A0A028E7D5 A0A069X5V4 A0A070FEI9 A0A070SGX9 A0A070UUQ8 A0A0A0FJ49 A0A0A8UIU5 A0A0E0U2S2
(71 more...)
Carboxylate reductase. [EC: 1.2.99.6]
An aldehyde + acceptor + H(2)O = a carboxylate + reduced acceptor.
  • Methylviologen can act as acceptor.
  • In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols.
 27 A0A069XIW3 A0A070SY73 A0A073G046 A0A074IA26 A0A080GAP2 A0A090HK67 A0A0E1LTW7 A0A0F6BZF3 A0A0M7MQK0 A0A1X3J5Z7
(17 more...)
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.
 24 A0A0E0QW39 A0A178WM01 C4NYZ3 G3X982 H9TB17 H9TB18 H9TB19 O54754 P48034 P80456
(14 more...)
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.
 7 A0A178WM01 O23887 O23888 Q7G191 Q7G192 Q7G193 Q7G9P4
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.
 6 P22985 P47989 P47990 P80457 Q00519 Q9MYW6
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.
 4 A0A0U3GXB0 M1I8F8 M1JFQ1 Q4J6M6
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.
 3 A0A1D9FFM2 O87681 U1ZW48
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.
 2 P19914 P19920
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.
 2 A0A1H3FYA8 Q0QLF4
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.
 2 A0A2R4BM78 O33820
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
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