CATH Classification

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.
Gottlieb, L., Marmorstein, R.
Structure
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