Function and Biology Details
Reaction catalysed:
Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-130811 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
N-terminal acetyltransferase A complex subunit nat1
Molecule details ›
Chains: A, B, C, D
Length: 734 amino acids
Theoretical weight: 84.15 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli
UniProt:
Sequence domains: N-terminal acetyltransferase A, auxiliary subunit
Structure domains:
Length: 734 amino acids
Theoretical weight: 84.15 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli
UniProt:
- Canonical:
O74985 (Residues: 1-729; Coverage: 100%)
Sequence domains: N-terminal acetyltransferase A, auxiliary subunit
Structure domains:
N-terminal acetyltransferase A complex catalytic subunit ard1
Molecule details ›
Chains: E, F, G, H
Length: 156 amino acids
Theoretical weight: 18.03 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli
UniProt:
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase
Length: 156 amino acids
Theoretical weight: 18.03 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli
UniProt:
- Canonical: Q9UTI3 (Residues: 1-156; Coverage: 88%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase
