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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_2_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 70084: N-terminal acetyltransferase complex ARD1 subunit

There are 3 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 amino-acid N(alpha)-acetyltransferase NatA. [EC: 2.3.1.255]
(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.
 34 A0A0D9R3B9 A0A0D9R3B9 A0A178UMY3 A0A178UMY3 A8W660 A8W660 F7GKG6 F7GKG6 G3R2U7 G3R2U7
(24 more...)
Transferred entry: 2.3.1.254, 2.3.1.255, 2.3.1.256, 2.3.1.257, 2.3.1.258 and 2.3.1.259. [EC: 2.3.1.88]
    		8 A0A0B2QKS6 A0A0B2QKS6 B9RVI5 B9RVI5 E0VIS6 E0VIS6 E3TGK5 E3TGK5
    Peptidylprolyl isomerase. [EC: 5.2.1.8]
    Peptidylproline (omega=180) = peptidylproline (omega=0).
    • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
    • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
    • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
    		 2 A0A161MQL0 A0A161MQL0
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