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CATH Superfamily 3.40.50.150

Vaccinia Virus protein VP39

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:

"
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 136367: Putative SAM-dependent methyltransferase

There are 5 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).
 90 A0A024KMW7 A0A024KMW7 A0A024L886 A0A024L886 A0A029JYA3 A0A029JYA3 A0A0E2KXP3 A0A0E2KXP3 A0A0G4JSN1 A0A0G4JSN1
(80 more...)
16S rRNA (adenine(1408)-N(1))-methyltransferase. [EC: 2.1.1.180]
S-adenosyl-L-methionine + adenine(1408) in 16S rRNA = S-adenosyl-L- homocysteine + N(1)-methyladenine(1408) in 16S rRNA.
  • The enzyme provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N(1)-methylation at position adenine(1408).
 6 A0A1M5JFD2 A0A1M5JFD2 P25920 P25920 Q2MEY3 Q2MEY3
Demethylrebeccamycin-D-glucose O-methyltransferase. [EC: 2.1.1.164]
4'-demethylrebeccamycin + S-adenosyl-L-methionine = rebeccamycin + S-adenosyl-L-homocysteine.
  • Catalyzes the last step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes.
  • The enzyme is able to use a wide variety substrates, tolerating variation on the imide heterocycle, deoxygenation of the sugar moiety, and even indolocarbazole glycoside anomers.
 2 A0A120CZG5 A0A120CZG5
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.
 2 A0A0J6D466 A0A0J6D466
Glycine/sarcosine N-methyltransferase. [EC: 2.1.1.156]
2 S-adenosyl-L-methionine + glycine = 2 S-adenosyl-L-homocysteine + N,N-dimethylglycine.
  • Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process.
  • This is the first enzyme and it leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of EC 2.1.1.157.
  • Differs from EC 2.1.1.20, as it can further methylate the product of the first reaction.
  • Acetate, dimethylglycine and S-adenosyl-L-homocysteine can inhibit the reaction.
 2 A0A1N6M6Y1 A0A1N6M6Y1
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