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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 70312: N-terminal acetyltransferase complex ARD1 subunit ...

There are 5 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 methionine N(alpha)-acetyltransferase NatB. [EC: 2.3.1.254]
(1) Acetyl-CoA + an N-terminal L-methionyl-L-asparaginyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-L-asparginyl-[protein] + CoA. (2) Acetyl-CoA + an N-terminal L-methionyl-L-glutaminyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-L-glutaminyl-[protein] + CoA. (3) Acetyl-CoA + an N-terminal L-methionyl-L-aspartyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein] + CoA. (4) Acetyl-CoA + an N-terminal L-methionyl-L-glutamyl-[protein] = an N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[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, and may also play a role in membrane targeting and gene silencing.
  • The NatB complex is found in all eukaryotic organisms, and specifically targets N-terminal L-methionine residues attached to Asn, Asp, Gln, or Glu residues at the second position.
  • Formerly EC 2.3.1.88.
 25 A0A087HKM3 A0A096NVP9 A0A0D9RGA5 A0A178WDM9 A0A1L8G1T6 B2GQZ5 D7KCB9 G3QNP5 G5CBB8 G7N327
(15 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]
    		20 A0A074SM21 A0A086JMJ9 A0A086KDL5 A0A086L9Q4 A0A086Q407 A0A086Q8X3 A0A0B2QEA6 A0A0B7FG96 A0A0K8RHP9 A0A125YX74
    (10 more...)
    Amino-acid N-acetyltransferase. [EC: 2.3.1.1]
    Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.
    • Also acts with L-aspartate and, more slowly, with some other amino acids.
    		 10 A0A024VE38 A0A024WXX5 A0A024XFH7 A0A060RRW7 A0A1J1HCB4 B0DQ76 Q8I249 W4IQ79 W7FMT3 W7JKG8
    Histone acetyltransferase. [EC: 2.3.1.48]
    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.
    		 8 A0A1A8X0X2 A0A1C3K9S5 A0A1C3KMN2 A0A1D3KWR2 B3NVQ9 B4PZF4 M9PI14 Q9VWF5
    Gluconokinase. [EC: 2.7.1.12]
    ATP + D-gluconate = ADP + 6-phospho-D-gluconate.
      		 1 A0A0D6LAB7
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