CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.470 |
Domain Context
CATH Clusters
| Superfamily | 3.30.70.470 |
| Functional Family |
Enzyme Information
| 2.8.4.1 |
Coenzyme-B sulfoethylthiotransferase.
based on mapping to UniProt Q49605
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 (2)
| Q49601 |
Q49601_9EURY
Methanopyrus kandleri
Methyl-coenzyme M reductase subunit beta
|
| Q49605 |
MCRA_METKA
Methanopyrus kandleri AV19
Methyl-coenzyme M reductase I subunit alpha
|
PDB Structure
| PDB | 1E6V |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Comparison of Three Methyl-Coenzyme M Reductases from Phylogenetically Distant Organisms: Unusual Amino Acid Modification, Conservation and Adaptation
J.Mol.Biol.
|
