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CATH Superfamily 3.50.50.60

FAD/NAD(P)-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:

"
FAD/NAD(P)-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 40: Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyl...

There are 1 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
Methylenetetrahydrofolate--tRNA-(uracil(54)-C(5))-methyltransferase (FADH(2)-oxidizing). [EC: 2.1.1.74]
5,10-methylenetetrahydrofolate + uracil(54) in tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA + FAD.
  • Up to 25% of the bases in mature tRNA are post-translationally modified or hypermodified.
  • One almost universal post-translational modification is the conversion of U54 into ribothymidine in the T-Psi-C loop, and this modification is found in most species studied to date.
  • Unlike this enzyme, which uses 5,10-methylenetetrahydrofolate and FADH(2) to supply the atoms for methylation of U54, EC 2.1.1.35 uses S-adenosyl-L-methionine.
  • Formerly EC 2.1.2.12.
 4148 A0A023PA82 A0A023PA82 A0A023PA82 A0A023PA82 A0A023PA82 A0A023PA82 A0A023PA82 A0A023PA82 A0A023PA82 A0A023PA82
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