CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1270 | Substrate Binding Domain Of Dnak; Chain:A; Domain 2 |
|
1.20.1270.30 |
Domain Context
CATH Clusters
| Superfamily | 1.20.1270.30 |
| Functional Family |
Enzyme Information
| 1.2.7.4 |
Anaerobic carbon-monoxide dehydrogenase.
based on mapping to UniProt P27989
CO + H(2)O + 2 oxidized ferredoxin = CO(2) + 2 reduced ferredoxin + 2 H(+).
-!- This prokaryotic enzyme catalyzes the reversible reduction of CO(2) to CO. -!- The electrons are transferred to redox proteins such as ferredoxin. -!- In purple sulfur bacteria and methanogenic archaea it catalyzes the oxidation of CO to CO(2), which is incorporated by the Calvin-Benson- Basham cycle or released, respectively. -!- In acetogenic and sulfate-reducing microbes it catalyzes the reduction of CO(2) to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, with which the enzyme forms a tight complex in those organisms. -!- In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2 which catalyze the overall reaction: CO + H(2)O = CO(2) + H(2). -!- Cf. EC 1.2.5.3. -!- Formerly EC 1.2.99.2.
|
UniProtKB Entries (1)
| P27988 |
DCMA_MOOTH
Moorella thermoacetica
Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha
|
PDB Structure
| PDB | 3I04 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase.
Biochemistry
|