View in Gene3D

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.
« Back to all FunFams

FunFam 14250: Zinc-type alcohol dehydrogenase YcjQ

There are 5 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(+).
 118 A0A027TRK4 A0A028AD34 A0A028E460 A0A029KX28 A0A070DAI0 A0A070FI50 A0A070KPB7 A0A070SQB0 A0A070V0E8 A0A073G991
(108 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.
 70 A0A029KX28 A0A070FI50 A0A070KPB7 A0A070SQB0 A0A070V0E8 A0A073G991 A0A073GRX7 A0A074I5M2 A0A074IM01 A0A080F833
(60 more...)
Alcohol dehydrogenase (NADP(+)). [EC: 1.1.1.2]
An alcohol + NADP(+) = an aldehyde + NADPH.
  • Some members of this group oxidize only primary alcohols; others act also on secondary alcohols.
  • May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55.
  • Re-specific with respect to NADPH.
 13 A0A0E1JB67 A0A0H0DKE9 A0A0J0FWC5 A0A0V9EDB6 A0A0W2HGT0 A0A144QJZ0 A0A144VGD9 A0A145G3H4 A0A155IKU8 A0A155VQZ1
(3 more...)
D-xylulose reductase. [EC: 1.1.1.9]
Xylitol + NAD(+) = D-xylulose + NADH.
  • Also acts as an L-erythrulose reductase.
 9 A0A0E2MDJ2 A0A0H3CJK6 A0A0J1Q3L4 A0A0M7BRZ2 A0A145PP96 A0A156SCC9 A0A169T624 A0A177JF03 A0A1B1JQD6
Alcohol dehydrogenase. [EC: 1.1.1.1]
(1) An alcohol + NAD(+) = an aldehyde or ketone + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
  • Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.
  • The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
 1 F5RXW5