CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.360 | Dihydrodipicolinate Reductase; domain 2 |
|
3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
Domain Context
CATH Clusters
| Superfamily | Dihydrodipicolinate Reductase; domain 2 |
| Functional Family |
Enzyme Information
| 1.2.1.75 |
Malonyl CoA reductase (malonate semialdehyde-forming).
based on mapping to UniProt Q96YK1
Malonate semialdehyde + CoA + NADP(+) = malonyl-CoA + NADPH.
-!- Catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles, autotrophic CO(2) fixation pathways found in some green non-sulfur phototrophic bacteria and some thermoacidophilic archaea, respectively. -!- The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits. -!- The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyzes the next reaction in the pathway, EC 1.1.1.298.
|
UniProtKB Entries (1)
| Q96YK1 |
MCR_SULTO
Sulfurisphaera tokodaii str. 7
Malonyl-CoA reductase
|
PDB Structure
| PDB | 4DPK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Basis for a Bispecific NADP+ and CoA Binding Site in an Archaeal Malonyl-Coenzyme A Reductase.
J.Biol.Chem.
|
