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CATH Superfamily 3.90.180.10

Medium-chain alcohol dehydrogenases, catalytic 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:

"
Medium-chain alcohol dehydrogenases, catalytic 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 2788: Alcohol dehydrogenase, zinc-dependent

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
Ribitol-5-phosphate 2-dehydrogenase. [EC: 1.1.1.137]
D-ribitol 5-phosphate + NAD(P)(+) = D-ribulose 5-phosphate + NAD(P)H.
  • The enzyme, characterized from the bacterium Lactobacillus plantarum, can use both NAD(+) and NADP(+) as electron acceptor (cf. EC 1.1.1.405).
 5 A0A0D5D0Q9 A0A0K6KBJ5 A0A0M0KR59 G4P1H6 Q8RKJ0
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(+).
 5 A0A0D5D0Q9 A0A0K6KBJ5 A0A0M0KR59 G4P1H6 Q8RKJ0