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 | Putative SAM-dependent methyltransferase |
Enzyme Information
| 2.1.1.64 |
3-demethylubiquinol 3-O-methyltransferase.
based on mapping to UniProt P39367
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).
|
| 2.1.1.- |
Methyltransferases.
based on mapping to UniProt P39367
|
UniProtKB Entries (1)
| P39367 |
YJHP_ECOLI
Escherichia coli K-12
Uncharacterized protein YjhP
|
PDB Structure
| PDB | 1NKV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
X-RAY STRUCTURE OF YJHP FROM E.COLI NORTHEAST STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NESG) TARGET ER13
To be published
|