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 named:

"
Glutaredoxin
".

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 79626: Type II iodothyronine deiodinase

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
Thyroxine 5'-deiodinase. [EC: 1.21.99.4]
3,5,3'-triiodo-L-thyronine + iodide + A + H(+) = L-thyroxine + AH(2).
  • The enzyme activity has only been demonstrated in the direction of 5'-deiodination, which renders the thyroid hormone more active.
  • The enzyme consists of type I and type II enzymes, both containing selenocysteine, but with different kinetics.
  • For the type I enzyme the first reaction is a reductive deiodination converting the -Se-H group of the enzyme into an -Se-I group; the reductant then reconverts this into -Se-H, releasing iodide.
  • Formerly EC 1.97.1.10 and EC 3.8.1.4.
44 A4GT88 A4GT88 L7WGA7 L7WGA7 O42411 O42411 O42449 O42449 P24389 P24389
(34 more...)
Thyroxine 5-deiodinase. [EC: 1.21.99.3]
3,3',5'-triiodo-L-thyronine + iodide + acceptor + H(+) = L-thyroxine + reduced acceptor.
  • The enzyme activity has only been demonstrated in the direction of 5-deiodination.
  • This removal of the 5-iodine, i.e. from the inner ring, largely inactivates the hormone thyroxine.
  • Formerly EC 1.97.1.11.
20 A7YD35 A7YD35 O42412 O42412 P49897 P49897 P49898 P49898 P49899 P49899
(10 more...)