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 | 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial |
Enzyme Information
| 2.1.1.201 |
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase.
based on mapping to UniProt P49017
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4- benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans- polyprenyl-1,4-benzoquinol.
-!- 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, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant. -!- The bifunctional enzyme from E.coli also catalyzes the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163).
|
UniProtKB Entries (1)
| P49017 |
COQ5_YEAST
Saccharomyces cerevisiae S288C
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
|
PDB Structure
| PDB | 4OBX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures and catalytic mechanism of the C-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway.
Acta Crystallogr.,Sect.D
|