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CATH Superfamily 1.10.45.10

Vanillyl-alcohol Oxidase; Chain A, domain 4

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:

"
Vanillyl-alcohol Oxidase; Chain A, domain 4
".

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 11 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
D-lactate dehydrogenase (cytochrome). [EC: 1.1.2.4]
(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+).
    		 20 A0A0L8VSA6 A0A178UIT0 A6ZXF3 A6ZXF7 B3LH58 B3LH62 C7GL20 C7GL24 C8Z6D0 G2WBY7
    (10 more...)
    Alkylglycerone-phosphate synthase. [EC: 2.5.1.26]
    1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion.
    • The ester-linked fatty acid of the substrate is cleaved and replaced by a long-chain alcohol in an ether linkage.
    		 9 A0A0B4JD21 O00116 O45218 O96759 O97157 P97275 Q8C0I1 Q9EQR2 Q9V778
    (R)-2-hydroxyglutarate--pyruvate transhydrogenase. [EC: 1.1.99.40]
    (R)-2-hydroxyglutarate + pyruvate = 2-oxoglutarate + (R)-lactate.
    • The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4 and is active with oxaloacetate as electron acceptor forming (R)-malate.
    		 8 A0A0L8VSA6 A6ZXF3 B3LH62 C7GL24 G2WBY7 N1PAJ9 P39976 P46681
    L-gulonolactone oxidase. [EC: 1.1.3.8]
    L-gulono-1,4-lactone + O(2) = L-ascorbate + H(2)O(2).
    • The product spontaneously isomerizes to L-ascorbate.
    • While most higher animals can synthesize ascorbic acid, primates and guinea pigs cannot.
    		 6 A0A480RSW6 P10867 P58710 Q3ZC33 Q8HXW0 Q90YK3
    D-2-hydroxyglutarate dehydrogenase. [EC: 1.1.99.39]
    (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor.
    • The enzyme has no activity with NAD(+) or NADP(+), and was assayed in vitro using artificial electron acceptors.
    • It has lower activity with (R)-lactate, (R)-2-hydroxybutyrate and meso-tartrate, and no activity with the (S) isomers.
    		 3 B8B7X6 O23240 Q7XI14
    4-methylphenol dehydrogenase (hydroxylating). [EC: 1.17.9.1]
    4-methylphenol + 4 oxidized azurin + H(2)O = 4-hydroxybenzaldehyde + 4 reduced azurin + 4 H(+).
    • This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit.
    • The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water.
    • The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm.
    • The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde.
    • Formerly EC 1.17.99.1.
    		 3 A0A077FEB1 P09788 R9WN81
    Alditol oxidase. [EC: 1.1.3.41]
    An alditol + O(2) = an aldose + H(2)O(2).
    • While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly.
    		 2 Q9KX73 Q9ZBU1
    Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase. [EC: 1.1.98.3]
    Trans,octacis-decaprenylphospho-beta-D-ribofuranose + FAD = trans,octacis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose + FADH(2).
    • The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.1.333 in the epimerization of trans,octacis-decaprenylphospho-beta-D-ribofuranose to trans,octacis- decaprenylphospho-beta-D-arabinofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
    		 1 A0R607
    D-arabinono-1,4-lactone oxidase. [EC: 1.1.3.37]
    D-arabinono-1,4-lactone + O(2) = dehydro-D-arabinono-1,4-lactone + H(2)O(2).
      		 1 Q9HDX8
      D-lactate dehydrogenase (acceptor). [EC: 1.1.99.6]
      (R)-lactate + acceptor = pyruvate + reduced acceptor.
      • The enzyme from the archaeon Archaeoglobus fulgidus cannot utilize NAD(+), cytochrome C, methylene blue or dimethylnaphthoquinone as acceptors.
      • In vitro it is active with artificial electron acceptors such as 2,6- dichlorophenolindophenol, but the physiological acceptor is not yet known.
      		 1 O29853
      Vanillyl-alcohol oxidase. [EC: 1.1.3.38]
      Vanillyl alcohol + O(2) = vanillin + H(2)O(2).
      • Converts a wide range of 4-hydroxybenzyl alcohols and 4-hydroxybenzylamines into the corresponding aldehydes.
      • The allyl group of 4-allylphenols is also converted into the -CH=CH-CH(2)OH group.
      		 1 P56216