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CATH Superfamily 3.40.630.30

Gcn5-related N-acetyltransferase (GNAT)

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 615: N-alpha-acetyltransferase 40

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
N-terminal L-serine N(alpha)-acetyltransferase NatD. [EC: 2.3.1.257]
(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.
 1 Q9USH6