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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like Domain

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:

"
NAD(P)-binding Rossmann-like 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 216520: Starvation sensing protein RspB

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
L-iditol 2-dehydrogenase. [EC: 1.1.1.14]
L-iditol + NAD(+) = L-sorbose + NADH.
  • This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals.
  • It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol.
  • Enzymes from different organisms or tissues display different substrate specificity.
  • The enzyme is specific to NAD(+) and can not use NADP(+).
 102 A0A066RDB9 A0A066RDB9 A0A069XJ29 A0A069XJ29 A0A070SUA9 A0A070SUA9 A0A080F6R0 A0A080F6R0 A0A0A0FFY3 A0A0A0FFY3
(92 more...)
L-threonine 3-dehydrogenase. [EC: 1.1.1.103]
L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH.
  • Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine.
  • This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex.
  • In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
 78 A0A027TZD8 A0A027TZD8 A0A028AKQ7 A0A028AKQ7 A0A028EAC9 A0A028EAC9 A0A070CFL2 A0A070CFL2 A0A073HE26 A0A073HE26
(68 more...)