Function and Biology Details
Reactions catalysed:
3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + trans-resveratrol + 4 CO(2)
ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA
Ferulic acid + CoA + ATP = feruloyl-CoA + products of ATP breakdown
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Thiolase-like
- Chalcone/stilbene synthase, C-terminal
- Chalcone/stilbene synthase, active site
- Chalcone/stilbene synthase, N-terminal
- AMP-binding enzyme, C-terminal domain
- AMP-binding enzyme, C-terminal domain superfamily
- AMP-binding, conserved site
- AMP-dependent synthetase/ligase domain
1 more domain
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-558029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-coumarate--CoA ligase 1; trihydroxystilbene synthase
Molecule details ›
Chain: A
Length: 979 amino acids
Theoretical weight: 106.63 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 979 amino acids
Theoretical weight: 106.63 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
- Canonical:
Q42524 (Residues: 1-561; Coverage: 100%) - Canonical: Q2HY10 (Residues: 1-392; Coverage: 100%)
Sequence domains:
- AMP-binding enzyme
- AMP-binding enzyme C-terminal domain
- Chalcone and stilbene synthases, N-terminal domain
- Chalcone and stilbene synthases, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P4122
Expression system: Escherichia coli
