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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 33947: Putative Glutathione-dependent formaldehyde dehydr...

There are 14 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.
    		 544 A0A023VFP3 A0A024GX47 A0A024H9V7 A0A031GA27 A0A031GBC3 A0A031GXL9 A0A031HRY3 A0A031J8R2 A0A060IA28 A0A061CXE7
    (534 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.
    		 217 A0A023B2Q7 A0A060DP24 A0A062BR30 A0A062BUK9 A0A069BBQ5 A0A075MNG0 A0A075UXC7 A0A076LZ92 A0A085H4V6 A0A089XE52
    (207 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.
    		 213 A0A009GCM1 A0A009SEK5 A0A024L5N9 A0A026V5B1 A0A027TF17 A0A029LVN6 A0A062IAW0 A0A066PCL9 A0A069XJP1 A0A070D5T9
    (203 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.
    		 137 A0A063XIY6 A0A075MNG0 A0A090D0U4 A0A0A0TNG7 A0A0B5P450 A0A0D1RHW1 A0A0D7XKJ6 A0A0D7XMF9 A0A0E1LLN0 A0A0F5RI59
    (127 more...)
    Transferred entry: 1.2.98.1. [EC: 1.2.99.4]
      		43 A0A0B7D8H5 A0A0B8XRL0 A0A0C7KBE9 A0A0D6H408 A0A0D6J2G9 A0A0D8FW21 A0A0D8HXM1 A0A0F0KKW2 A0A0F0KXS4 A0A0F2C5F5
      (33 more...)
      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.
      		 3 F5RUB0 F5SKF8 F9DTL1
      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(+).
      		 3 A0A0E2ZPR6 B2AIN0 Q3JDI5
      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 A0A162TE25 A0A1E7X4D1
      (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 A0A162TE25 A0A1E7X4D1
      L-arabinose 1-dehydrogenase. [EC: 1.1.1.46]
      L-arabinose + NAD(+) = L-arabinono-1,4-lactone + NADH.
        		 2 I4ETW2 I4EVN7
        Transferred entry: 1.1.1.284 and 4.4.1.22. [EC: 1.2.1.1]
          		2 Q5P6L9 Q7UKC0
          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.
          		 1 C4WPF4
          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.
          		 1 A0A151AGA2
          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.
          		 1 A0A151AGN7
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