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CATH Superfamily 1.10.10.10

Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

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 named:

"
Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
".

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 358: Acetylserotonin O-methyltransferase

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
Acetylserotonin O-methyltransferase. [EC: 2.1.1.4]
S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin.
  • Some other hydroxyindoles also act as acceptor, more slowly.
 10 B3GSH5 D3KU66 D3KU67 P10950 P46597 P46597 Q8HZJ0 Q92056 X5D2A4 X5D2A4
Nucleotide diphosphatase. [EC: 3.6.1.9]
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate.
  • The enzyme preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates.
  • In vitro the enzyme also acts as a nucleotidohydrolase on ADP, NAD(+), NADP(+), FAD, and CoA.
  • Formerly EC 3.6.1.19.
 1 O95671
3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase. [EC: 2.1.1.302]
S-adenosyl-L-methionine + 3-hydroxy-5-methyl-1-naphthoate = S-adenosyl-L- homocysteine + 3-methoxy-5-methyl-1-naphthoate.
  • The enzyme from the bacterium Streptomyces sahachiroi is involved in the biosynthesis of 3-methoxy-5-methyl-1-naphthoate, a component of of the the antitumor antibiotic azinomycin B.
 1 B4XY98
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