CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1260 | Ferritin |
|
1.20.1260.10 | Ferritin, core subunit, four-helix bundle |
Domain Context
CATH Clusters
| Superfamily | 1.20.1260.10 |
| Functional Family |
Enzyme Information
| 4.1.99.5 |
Aldehyde oxygenase (deformylating).
based on mapping to UniProt Q7V6D4
A long-chain aldehyde + O(2) + 2 NADPH = an alkane + formate + H(2)O + 2 NADP(+).
-!- Involved in the biosynthesis of alkanes. -!- The enzyme from the cyanobacterium Nostoc punctiforme PCC 73102 is only active in vitro in the presence of ferredoxin, ferredoxin reductase and NADPH, and produces mostly C(15) to C(17) alkanes. -!- The enzyme from pea (Pisum sativum) produces alkanes of chain length C18 to C32 and is inhibited by metal-chelating agents. -!- The substrate for this enzyme is formed by EC 1.2.1.80.
|
UniProtKB Entries (1)
| Q7V6D4 |
ALDEC_PROMM
Prochlorococcus marinus str. MIT 9313
Aldehyde decarbonylase
|
PDB Structure
| PDB | 4PGI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound.
Acs Chem.Biol.
|
