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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 8504: Zinc-containing alcohol dehydrogenase NAD-dependen...

There are 3 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
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.
 42 A0A045J2Y2 A0A049DW48 A0A083WI98 A0A0E2WB87 A0A0E2WZ66 A0A0E2XC43 A0A0G4DUB3 A0A0H2ZXU2 A0A0H3LD95 A0A0H3MB17
(32 more...)
Alcohol dehydrogenase (nicotinoprotein). [EC: 1.1.99.36]
Ethanol + acceptor = acetaldehyde + reduced acceptor.
  • Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD(+)/NADH cofactor that does not dissociate during the catalytic process.
  • Instead, the cofactor is regenerated by a second substrate or electron carrier.
  • While the in vivo electron acceptor is not known, N,N-dimethyl-4- nitrosoaniline (NDMA) can serve this function in vitro.
  • The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol.
 34 A0A049DW48 A0A081I1Y3 A0A0E2WB87 A0A0E2WZ66 A0A0E2XC43 A0A0H2ZXU2 A0A0P7IAH7 A0A164FXB6 A0A1A2F4Z8 A0A1B9CC63
(24 more...)
S-(hydroxymethyl)glutathione dehydrogenase. [EC: 1.1.1.284]
S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H.
  • The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22.
  • Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC 3.1.2.12.
  • Also specifically reduces S-nitrosylglutathione.
  • Formerly EC 1.2.1.1.
 20 A0A045J2Y2 A0A083WI98 A0A0G4DUB3 A0A0H3LD95 A0A0H3MB17 A0A0K2HT32 A0A109SL57 A0A109SUJ4 A0A197J0L0 A0A1K3A7Q1
(10 more...)