Function and Biology Details
Reaction catalysed:
An N-acyl-L-homoserine lactone + H(2)O = L-homoserine lactone + a carboxylate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191265 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acyl-homoserine lactone acylase PvdQ subunit alpha
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 18.59 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli str. K-12 substr. DH10B
UniProt:
Structure domains: Penicillin Amidohydrolase, domain 1
Length: 170 amino acids
Theoretical weight: 18.59 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli str. K-12 substr. DH10B
UniProt:
- Canonical:
Q9I194 (Residues: 24-193; Coverage: 23%)
Structure domains: Penicillin Amidohydrolase, domain 1
Acyl-homoserine lactone acylase PvdQ subunit beta
Molecule details ›
Chain: B
Length: 546 amino acids
Theoretical weight: 60.49 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli str. K-12 substr. DH10B
UniProt:
Sequence domains: Penicillin amidase
Structure domains:
Length: 546 amino acids
Theoretical weight: 60.49 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli str. K-12 substr. DH10B
UniProt:
- Canonical: Q9I194 (Residues: 217-762; Coverage: 74%)
Sequence domains: Penicillin amidase
Structure domains:
