Function and Biology Details
Reactions catalysed:
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA
A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
- 3-hydroxyacyl-CoA dehydrogenase, C-terminal
- 3-hydroxyacyl-CoA dehydrogenase, conserved site
- 3-hydroxyacyl-CoA dehydrogenase, NAD binding
- NAD(P)-binding domain superfamily
- Enoyl-CoA hydratase/isomerase, conserved site
- Enoyl-CoA hydratase/isomerase
- ClpP/crotonase-like domain superfamily
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
Molecule details ›
Chain: A
Length: 725 amino acids
Theoretical weight: 78.94 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 725 amino acids
Theoretical weight: 78.94 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9ZPI5 (Residues: 1-725; Coverage: 100%)
Sequence domains:
- Enoyl-CoA hydratase/isomerase
- 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain
- 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
BESSY BEAMLINE 14.1
Spacegroup:
P3221
Expression system: Escherichia coli BL21(DE3)
