Function and Biology Details
Reactions catalysed:
(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Semialdehyde dehydrogenase, NAD-binding
- Acetaldehyde dehydrogenase
- Pyruvate carboxyltransferase
- 4-hydroxy-2-oxovalerate aldolase
- Acetaldehyde dehydrogenase, C-terminal
- NAD(P)-binding domain superfamily
- DmpG-like communication
- 4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain
1 more domain
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-156283 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
4-hydroxy-2-oxovalerate aldolase
Molecule details ›
Chains: A, C, E, G
Length: 345 amino acids
Theoretical weight: 37.52 KDa
Source organism: Pseudomonas sp. CF600
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 345 amino acids
Theoretical weight: 37.52 KDa
Source organism: Pseudomonas sp. CF600
Expression system: Escherichia coli
UniProt:
- Canonical:
P51016 (Residues: 1-345; Coverage: 100%)
Sequence domains:
Structure domains:
Acetaldehyde dehydrogenase
Molecule details ›
Chains: B, D, F, H
Length: 312 amino acids
Theoretical weight: 32.71 KDa
Source organism: Pseudomonas sp. CF600
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 312 amino acids
Theoretical weight: 32.71 KDa
Source organism: Pseudomonas sp. CF600
Expression system: Escherichia coli
UniProt:
- Canonical: Q52060 (Residues: 1-312; Coverage: 100%)
Sequence domains:
Structure domains:
