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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 34068: Oxidoreductase, zinc-binding dehydrogenase family

There are 9 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.
 114 A0A077UUE8 A0A077UUE8 A0A090NB76 A0A090NB76 A0A095HH48 A0A095HH48 A0A0A6ZTC3 A0A0A6ZTC3 A0A0B6XSJ7 A0A0B6XSJ7
(104 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.
 92 A0A089QBS7 A0A089QBS7 A0A0E1AKN8 A0A0E1AKN8 A0A0H2VHL1 A0A0H2VHL1 A0A0H2WZ89 A0A0H2WZ89 A0A0H2XIR0 A0A0H2XIR0
(82 more...)
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).
 76 A0A083UDQ8 A0A083UDQ8 A0A099K9Q3 A0A099K9Q3 A0A099KYZ3 A0A099KYZ3 A0A099LJ16 A0A099LJ16 A0A0B2R8L6 A0A0B2R8L6
(66 more...)
Curcumin reductase. [EC: 1.3.1.n3]
Tetrahydrocurcumin + 2 NADP(+) = curcumin + 2 NADPH.
  • The enzyme, from the bacterium Escherichia coli is also active with 3-octene-2-one (59.7%), 3-hepten-2-one (28%), and resveratrol (14.8%).
 36 A0A037YEC2 A0A037YEC2 A0A069XFY2 A0A069XFY2 A0A070UZ02 A0A070UZ02 A0A074IJU9 A0A074IJU9 A0A0E1LWX3 A0A0E1LWX3
(26 more...)
15-oxoprostaglandin 13-reductase. [EC: 1.3.1.48]
11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)(+) = (5Z)-(13E)-11- alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.
  • Reduces 15-oxoprostaglandins to 13,14-dihydro derivatives.
  • The enzyme from placenta is specific for NAD(+).
 20 A0A0A0G349 A0A0A0G349 A0A0M7MUW1 A0A0M7MUW1 H2Q8K7 H2Q8K7 L8IN04 L8IN04 Q32L99 Q32L99
(10 more...)
Delta(4)-3-oxosteroid 5-beta-reductase. [EC: 1.3.1.3]
(1) 5-beta-cholestan-3-one + NADP(+) = cholest-4-en-3-one + NADPH. (2) 17,21-dihydroxy-5-beta-pregnane-3,11,20-trione + NADP(+) = cortisone + NADPH.
  • The enzyme from human efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites; it can also act on aldosterone, corticosterone and cortisol, but to a lesser extent.
  • The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3- one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates.
 4 S0AJ59 S0AJ59 S4YK04 S4YK04
(+)-pulegone reductase. [EC: 1.3.1.81]
(1) (-)-menthone + NADP(+) = (+)-pulegone + NADPH. (2) (+)-isomenthone + NADP(+) = (+)-pulegone + NADPH.
  • NADH cannot replace NADPH as reductant.
  • The Delta(8,9)-double bond of (+)-cis-isopulegone and the Delta(1,2)- double bond of (+-)-piperitone are not substrates.
  • The enzyme from peppermint (Mentha x piperita) converts (+)-pulegone into both (-)-menthone and (+)-isomenthone at a ratio of 70:30 for native enzyme but it does not catalyze the reverse reaction.
 2 Q6WAU0 Q6WAU0
2-alkenal reductase (NADP(+)). [EC: 1.3.1.102]
An n-alkanal + NADP(+) = an alk-2-enal + NADPH.
  • Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones.
  • Has very low activity with NAD as reductant (cf. EC 1.3.1.74).
 2 Q9SLN8 Q9SLN8
Protein-N(pi)-phosphohistidine--D-mannose phosphotransferase. [EC: 2.7.1.191]
[Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L- histidine + D-mannose 6-phosphate(Side 2).
  • This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS).
  • The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it.
  • The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9.
  • Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency.
  • The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate.
  • Formerly EC 2.7.1.69.
 2 A0A1D4PNH5 A0A1D4PNH5