CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.390 | Methyl-coenzyme M Reductase; Chain A, domain 1 |
|
3.90.390.10 | Methyl-coenzyme M Reductase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Methyl-coenzyme M Reductase; Chain A, domain 1 |
| Functional Family |
Enzyme Information
| 2.8.4.1 |
Coenzyme-B sulfoethylthiotransferase.
based on mapping to UniProt P11558
Methyl-CoM + CoB = CoM-S-S-CoB + methane.
-!- This enzyme catalyzes the final step in methanogenesis, the biological production of methane. -!- This important anaerobic process is carried out only by methanogenic archaea. -!- The enzyme can also function in reverse, for anaerobic oxidation of methane. -!- The enzyme requires the hydroporphinoid nickel complex coenzyme F(430). -!- Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. -!- The sulfide sulfur can be replaced by selenium but not by oxygen.
|
UniProtKB Entries (1)
| P11558 |
MCRA_METTM
Methanothermobacter marburgensis str. Marburg
Methyl-coenzyme M reductase I subunit alpha
|
PDB Structure
| PDB | 1HBN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
On the Mechanism of Biological Methane Formation: Structural Evidence for Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding
J.Mol.Biol.
|
