CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.630 | Aminopeptidase |
|
3.40.630.30 | Gcn5-related N-acetyltransferase (GNAT) |
Domain Context
CATH Clusters
| Superfamily | 3.40.630.30 |
| Functional Family |
Enzyme Information
| 2.3.1.257 |
N-terminal L-serine N(alpha)-acetyltransferase NatD.
based on mapping to UniProt Q9USH6
(1) Acetyl-CoA + an N-terminal-L-seryl-[histone H4] = an N-terminal- N(alpha)-acetyl-L-seryl-[histone H4] + CoA. (2) Acetyl-CoA + an N-terminal-L-seryl-[histone H2A] = an N-terminal- N(alpha)-acetyl-L-seryl-[histone H2A] + CoA.
-!- N-terminal-acetylases (NATs) catalyze the covalent attachment of an acetyl moiety from acetyl-CoA to the free alpha-amino group at the N-terminus of a protein. -!- This irreversible modification neutralizes the positive charge at the N-terminus and makes the N-terminal residue larger and more hydrophobic. -!- NatD is found in all eukaryotic organisms, and acetylates solely the serine residue at the N-terminus of histones H2A or H4. -!- Efficient recognition and acetylation by NatD requires at least the first 30 to 50 highly conserved amino acid residues of the histone N terminus. -!- Formerly EC 2.3.1.88.
|
UniProtKB Entries (1)
| Q9USH6 |
NAA40_SCHPO
Schizosaccharomyces pombe 972h-
N-alpha-acetyltransferase 40
|
PDB Structure
| PDB | 4UA3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Molecular Basis for Histone H4- and H2A-Specific Amino-Terminal Acetylation by NatD.
Structure
|
