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 | N-alpha-acetyltransferase 10 isoform X1 |
Enzyme Information
| 2.3.1.255 |
N-terminal amino-acid N(alpha)-acetyltransferase NatA.
based on mapping to UniProt P41227
(1) Acetyl-CoA + an N-terminal-glycyl-[protein] = an N-terminal-N(alpha)- acetyl-glycyl-[protein] + CoA. (2) Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal- N(alpha)-acetyl-L-alanyl-[protein] + CoA. (3) Acetyl-CoA + an N-terminal-L-seryl-[protein] = an N-terminal- N(alpha)-acetyl-L-seryl-[protein] + CoA. (4) Acetyl-CoA + an N-terminal-L-valyl-[protein] = an N-terminal- N(alpha)-acetyl-L-valyl-[protein] + CoA. (5) Acetyl-CoA + an N-terminal-L-cysteinyl-[protein] = an N-terminal- N(alpha)-acetyl-L-cysteinyl-[protein] + CoA. (6) Acetyl-CoA + an N-terminal-L-threonyl-[protein] = an N-terminal- N(alpha)-acetyl-L-threonyl-[protein] + 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. -!- The NatA complex is found in all eukaryotic organisms, and specifically targets N-terminal Ala, Gly, Cys, Ser, Thr, and Val residues, that became available after removal of the initiator methionine. -!- Formerly EC 2.3.1.88.
|
UniProtKB Entries (1)
| Q9BXJ9 |
NAA15_HUMAN
Homo sapiens
N-alpha-acetyltransferase 15, NatA auxiliary subunit
|
PDB Structure
| PDB | 6C9M |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK.
Structure
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