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 60 isoform X1 |
Enzyme Information
| 2.3.1.48 |
Histone acetyltransferase.
based on mapping to UniProt Q9H7X0
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine.
-!- A group of enzymes acetylating histones. -!- Several of the enzymes can also acetylate lysines in other proteins.
|
| 2.3.1.259 |
N-terminal methionine N(alpha)-acetyltransferase NatF.
based on mapping to UniProt Q9H7X0
Acetyl-CoA + an N-terminal-L-methionyl-[transmembrane protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-[transmembrane 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, makes the N-terminal residue larger and more hydrophobic, and prevents its removal by hydrolysis. -!- NatF is found only in higher eukaryotes, and is absent from yeast. -!- Unlike other Nat systems the enzyme is located in the Golgi apparatus. -!- It faces the cytosolic side of intracellular membranes, and specifically acetylates transmembrane proteins whose N termini face the cytosol. -!- NatF targets N-terminal L-methionine residues attached to Lys, Ser, Val, Leu, Gln, Ile, Tyr and Thr residues. -!- Formerly EC 2.3.1.88.
|
UniProtKB Entries (1)
| Q9H7X0 |
NAA60_HUMAN
Homo sapiens
N-alpha-acetyltransferase 60
|
PDB Structure
| PDB | 5ICW |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of the Golgi-Associated Human N alpha-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific Acetylation.
Structure
|
