CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.630.30
Functional Family N-alpha-acetyltransferase 60 isoform X1

Enzyme Information
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.
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

UniProtKB Entries (1)

Homo sapiens
N-alpha-acetyltransferase 60

PDB Structure

External Links
Primary Citation
Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase
Chen, J.Y., Liu, L., Cao, C.L., Li, M.J., Tan, K., Yang, X., Yun, C.H.
Sci Rep