Function and Biology Details
Reaction catalysed:
CoA-(4'-phosphopantetheine) + an apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + an [acyl-carrier-protein]
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128245 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrocidine synthase 3
Molecule details ›
Chain: C
Length: 90 amino acids
Theoretical weight: 9.97 KDa
Source organism: Brevibacillus parabrevis
Expression system: Escherichia coli
UniProt:
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like
Length: 90 amino acids
Theoretical weight: 9.97 KDa
Source organism: Brevibacillus parabrevis
Expression system: Escherichia coli
UniProt:
- Canonical:
O30409 (Residues: 3038-3113; Coverage: 1%)
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like
4'-phosphopantetheinyl transferase Sfp
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 27.25 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain
Length: 232 amino acids
Theoretical weight: 27.25 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
- Canonical: P39135 (Residues: 1-224; Coverage: 100%)
Sequence domains: 4'-phosphopantetheinyl transferase superfamily
Structure domains: 4'-phosphopantetheinyl transferase domain
