CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.140 | 8 Propeller |
|
2.140.10 | Methanol Dehydrogenase; Chain A |
|
2.140.10.10 | Quinoprotein alcohol dehydrogenase-like superfamily |
Domain Context
CATH Clusters
| Superfamily | Quinoprotein alcohol dehydrogenase-like superfamily |
| Functional Family |
Enzyme Information
| 1.1.9.1 |
Alcohol dehydrogenase (azurin).
based on mapping to UniProt Q46444
A primary alcohol + azurin = an aldehyde + reduced azurin.
-!- Occurs in Comamonas and Pseudomonas. -!- Does not require an amine activator. -!- Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate. -!- Usually assayed with phenazine methosulfate or ferricyanide. -!- Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. -!- Formerly EC 1.1.98.1.
|
UniProtKB Entries (1)
| Q46444 |
QHED_COMTE
Comamonas testosteroni
Quinohemoprotein alcohol dehydrogenase
|
PDB Structure
| PDB | 1KB0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer.
J.Biol.Chem.
|
