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:

"
Vaccinia Virus protein VP39
".

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 28: Ubiquinone biosynthesis O-methyltransferase

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
3-demethylubiquinol 3-O-methyltransferase. [EC: 2.1.1.64]
S-adenosyl-L-methionine + 3-demethylubiquinone-n = S-adenosyl-L- homocysteine + ubiquinone-n.
  • This enzyme is involved in ubiquinone biosynthesis.
  • Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units.
  • However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units.
  • For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast.
  • The enzymes from yeast, Escherichia coli and rat also catalyze the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reaction that is classified as EC 2.1.1.114).
7592 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0
(7582 more...)
2-polyprenyl-6-hydroxyphenol methylase. [EC: 2.1.1.222]
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol.
  • UbiG catalyzes both methylation steps in ubiquinone biosynthesis in Escherichia coli.
  • The second methylation is classified as EC 2.1.1.64.
  • In eukaryotes Coq3 catalyzes the two methylation steps in ubiquinone biosynthesis.
  • However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114.
  • The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans- polyprenylbenzoate) differs by an additional carboxylate moiety.
7590 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0 A0A023YZV0
(7580 more...)
Polyprenyldihydroxybenzoate methyltransferase. [EC: 2.1.1.114]
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate = S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans- polyprenylbenzoate.
  • This enzyme is involved in ubiquinone biosynthesis.
  • Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone- 9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units.
  • However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units.
  • For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast.
  • The enzymes from yeast and rat also catalyze the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively (this activity is classified as EC 2.1.1.64).
2 O74421 Q54XD0
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