View in Gene3D

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.
« Back to all FunFams

FunFam 291888: Glutathione-independent formaldehyde dehydrogenase

There are 11 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
Formaldehyde dehydrogenase. [EC: 1.2.1.46]
Formaldehyde + NAD(+) + H(2)O = formate + NADH.
    		 670 A0A024GX47 A0A024GX47 A0A024H9V7 A0A024H9V7 A0A031GA27 A0A031GA27 A0A031GBC3 A0A031GBC3 A0A031GXL9 A0A031GXL9
    (660 more...)
    Formaldehyde dismutase. [EC: 1.2.98.1]
    2 formaldehyde + H(2)O = formate + methanol.
    • Enzyme-bound NADPH formed by oxidation of formaldehyde to formate is oxidized back to NADP(+) by reaction with a second formaldehyde, yielding methanol.
    • The enzyme from Mycobacterium sp. DSM 3803 also catalyzes the reactions of EC 1.1.99.36 and EC 1.1.99.37.
    • Formaldehyde and acetaldehyde can act as donors; formaldehyde, acetaldehyde and propanal can act as acceptors.
    • Formerly EC 1.2.99.4.
    		 322 A0A009GCM1 A0A009GCM1 A0A009SEK5 A0A009SEK5 A0A024L5N9 A0A024L5N9 A0A026V5B1 A0A026V5B1 A0A027TF17 A0A027TF17
    (312 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.
    		 104 A0A062BR30 A0A062BR30 A0A062BUK9 A0A062BUK9 A0A077SHR2 A0A077SHR2 A0A085H4V6 A0A085H4V6 A0A0E1CKU7 A0A0E1CKU7
    (94 more...)
    Transferred entry: 1.2.98.1. [EC: 1.2.99.4]
      		46 A0A0B7D8H5 A0A0B7D8H5 A0A0C7KBE9 A0A0C7KBE9 A0A0D6H408 A0A0D6H408 A0A0D8FW21 A0A0D8FW21 A0A0F6AYA6 A0A0F6AYA6
      (36 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.
      		 28 A0A063XIY6 A0A063XIY6 A0A0T8KV54 A0A0T8KV54 A0A0T8Q0M2 A0A0T8Q0M2 A0A0W0VAI1 A0A0W0VAI1 A0A1C3TRA8 A0A1C3TRA8
      (18 more...)
      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(+).
      		 6 A0A0E7TZN2 A0A0E7TZN2 A0A0H3LA90 A0A0H3LA90 Q7D7T9 Q7D7T9
      Kynurenine--oxoglutarate transaminase. [EC: 2.6.1.7]
      L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
      • Also acts on 3-hydroxykynurenine.
      • The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
      		 2 C4WPF4 C4WPF4
      S-(hydroxymethyl)glutathione synthase. [EC: 4.4.1.22]
      S-(hydroxymethyl)glutathione = glutathione + formaldehyde.
      • The enzyme from Paracoccus denitrificans accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, in the formaldehyde- detoxification pathway.
      • Formerly EC 1.2.1.1.
      		 2 F5RUB0 F5RUB0
      Aldehyde dehydrogenase (NAD(+)). [EC: 1.2.1.3]
      An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH.
      • Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
      • Formerly EC 1.1.1.70.
      		 2 A0A1E7VQ93 A0A1E7VQ93
      Succinate-semialdehyde dehydrogenase (acetylating). [EC: 1.2.1.76]
      Succinate semialdehyde + CoA + NADP(+) = succinyl-CoA + NADPH.
      • Catalyzes the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde.
      • The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation, and in Metallosphaera sedula, where it participates in the 3-hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO(2) fixation pathway found in some thermoacidophilic archaea.
      		 2 A0A151AGN7 A0A151AGN7
      (R,R)-butanediol dehydrogenase. [EC: 1.1.1.4]
      (R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH.
      • Also converts diacetyl into acetoin with NADH as reductant.
      		 2 A0A1E7VQ93 A0A1E7VQ93