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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 1051: Carminomycin 4-O-methyltransferase DnrK

There are 2 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
Carminomycin 4-O-methyltransferase. [EC: 2.1.1.292]
S-adenosyl-L-methionine + carminomycin = S-adenosyl-L-homocysteine + daunorubicin.
  • The enzymes from the Gram-positive bacteria Streptomyces sp. C5 and Streptomyces peucetius are involved in the biosynthesis of the anthracycline daunorubicin.
  • In vitro the enzyme from Streptomyces sp. C5 also catalyzes the 4-O- methylation of 13-dihydrocarminomycin, rhodomycin D and 10-carboxy- 13-deoxycarminomycin.
 5 A0A2D3UDR4 A0A2D3UDR4 Q06528 Q06528 Q55216
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase. [EC: 2.1.1.303]
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate.
  • The enzyme from the bacterium Streptomyces carzinostaticus is involved in the biosynthesis of 2-hydroxy-7-methoxy-5-methyl-1- naphthoate.
  • This compound is part of the enediyne chromophore of the antitumor antibiotic neocarzinostatin.
  • In vivo the enzyme catalyzes the regiospecific methylation at the 7-hydroxy group of its native substrate 2,7-dihydroxy-5-methyl-1- naphthoate.
  • In vitro it also recognizes other dihydroxynaphthoic acids and catalyzes their regiospecific O-methylation.
 1 Q84HC8