CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.50 | Rossmann fold | |
3.40.50.150 | Vaccinia Virus protein VP39 |
Domain Context
CATH Clusters
Superfamily | Vaccinia Virus protein VP39 |
Functional Family |
Enzyme Information
2.1.1.222 |
2-polyprenyl-6-hydroxyphenol methylase.
based on mapping to UniProt A8A296
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.
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2.1.1.64 |
3-demethylubiquinol 3-O-methyltransferase.
based on mapping to UniProt A8A296
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).
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UniProtKB Entries (1)
A8A296 |
UBIG_ECOHS
Escherichia coli HS
Ubiquinone biosynthesis O-methyltransferase
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PDB Structure
PDB | 5DPM |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal structure of UbiG mutant in complex with SAH at 2.1 angstroms resolution
To Be Published
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