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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 290191: Putative quinone oxidoreductase YhdH

There are 4 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
Acrylyl-CoA reductase (NADPH). [EC: 1.3.1.84]
Propanoyl-CoA + NADP(+) = acrylyl-CoA + NADPH.
  • Catalyzes a step in the 3-hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO(2) fixation pathway found in some thermoacidophilic archaea.
  • The reaction is catalyzed in the opposite direction to that shown.
  • The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA.
  • Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16.
 294 A0A021X315 A0A021X315 A0A069XU36 A0A069XU36 A0A070SYS4 A0A070SYS4 A0A070UME2 A0A070UME2 A0A074IFB0 A0A074IFB0
(284 more...)
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.
 232 A0A017HEC6 A0A017HEC6 A0A023Z391 A0A023Z391 A0A025CHJ8 A0A025CHJ8 A0A063Y9A4 A0A063Y9A4 A0A064DLG0 A0A064DLG0
(222 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.
 80 A0A069XU36 A0A069XU36 A0A070SYS4 A0A070SYS4 A0A070UME2 A0A070UME2 A0A074IFB0 A0A074IFB0 A0A077ZLW6 A0A077ZLW6
(70 more...)
NADPH:quinone reductase. [EC: 1.6.5.5]
NADPH + 2 quinone = NADP(+) + 2 semiquinone.
  • Specific for NADPH.
  • Catalyzes the one-electron reduction of certain quinones, with the orthoquinones 1,2-naphthoquinone and 9,10-phenanthrenequinone being the best substrates.
  • Dicoumarol (cf. EC 1.6.5.2) and nitrofurantoin are competitive inhibitors with respect to the quinone substrate.
  • The semiquinone free-radical product may be non-enzymically reduced to the hydroquinone or oxidized back to quinone in the presence of O(2).
  • Abundant in the lens of the eye of some mammalian species.
 10 A0A0T8FGQ4 A0A0T8FGQ4 E3HJ13 E3HJ13 I2C1Z6 I2C1Z6 Q2RQ38 Q2RQ38 Q39AZ5 Q39AZ5
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