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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 291092: Quinone oxidoreductase 1

There are 7 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
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.
 2100 A0A011MZJ9 A0A011MZJ9 A0A011NXI1 A0A011NXI1 A0A011P596 A0A011P596 A0A011PPC7 A0A011PPC7 A0A011QD01 A0A011QD01
(2090 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.
 4 K0KNP5 K0KNP5 K0KRU4 K0KRU4
2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
  • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
  • Alk-2-enals of shorter chain have lower affinities.
  • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
  • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
 2 A0A060TAN2 A0A060TAN2
L-lactate dehydrogenase. [EC: 1.1.1.27]
(S)-lactate + NAD(+) = pyruvate + NADH.
  • Also oxidizes other (S)-2-hydroxymonocarboxylic acids.
  • NADP(+) acts, more slowly, with the animal, but not the bacterial, enzyme.
 2 G8PX85 G8PX85
Geraniol dehydrogenase (NAD(+)). [EC: 1.1.1.347]
Geraniol + NAD(+) = geranial + NADH.
  • The enzyme from the bacterium Castellaniella defragrans is most active in vitro with perillyl alcohol.
  • The enzyme from the prune mite Carpoglyphus lactis also acts (more slowly) on farnesol but not on nerol.
  • Formerly EC 1.1.1.n14.
 2 A0A084FZJ5 A0A084FZJ5
DNA-3-methyladenine glycosylase I. [EC: 3.2.2.20]
Hydrolysis of alkylated DNA, releasing 3-methyladenine.
    		 2 G8PX85 G8PX85
    Perillyl-alcohol dehydrogenase. [EC: 1.1.1.144]
    Perillyl alcohol + NAD(+) = perillyl aldehyde + NADH.
    • Oxidizes a number of primary alcohols with the alcohol group allylic to an endocyclic double bond and a 6-membered ring, either aromatic or hydroaromatic.
    		 2 A0A084FZJ5 A0A084FZJ5