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CATH Superfamily 3.20.20.100

NADP-dependent oxidoreductase domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
NADP-dependent oxidoreductase 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 9: Aldo-keto reductase family 1 member B1

There are 5 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
Aldehyde reductase. [EC: 1.1.1.21]
Alditol + NAD(P)(+) = aldose + NAD(P)H.
  • Wide specificity.
  • Formerly EC 1.1.1.139.
 22 A0A024R7A8 A0A024R7A8 G3IE21 G3IE21 O08782 O08782 P07943 P15121 P15121 P15122
(12 more...)
Allyl-alcohol dehydrogenase. [EC: 1.1.1.54]
Allyl alcohol + NADP(+) = acrolein + NADPH.
  • Also acts on saturated primary alcohols.
 13 A0A024R7A8 A0A024R7A8 O60218 P07943 P15121 P15121 P15122 P16116 P45376 P45376
(3 more...)
NADP-retinol dehydrogenase. [EC: 1.1.1.300]
All-trans-retinol + NADP(+) = all-trans-retinal + NADPH.
  • Greater catalytic efficiency in the reductive direction.
  • This observation, and the enzyme's localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary beta-carotene by EC 1.13.11.63.
  • Km-values for NADP(+) and NADPH are at least 800-fold lower than those for NAD(+) and NADH.
  • This enzyme differs from EC 1.1.1.105 which prefers NAD(+) and NADH.
  • Formerly EC 1.1.1.n2.
 13 A0A024R7A8 A0A024R7A8 O60218 P07943 P15121 P15121 P15122 P16116 P45376 P45376
(3 more...)
D/L-glyceraldehyde reductase. [EC: 1.1.1.372]
(1) Glycerol + NADP(+) = L-glyceraldehyde + NADPH. (2) Glycerol + NADP(+) = D-glyceraldehyde + NADPH.
  • The enzyme takes part in a D-galacturonate degradation pathway in the fungi Aspergillus niger and Trichoderma reesei (Hypocrea jecorina).
  • It has equal activity with D- and L-glyceraldehyde, and can also reduce glyoxal and methylglyoxal.
  • The reaction is only observed in the direction of glyceraldehyde reduction.
 12 A0A024R7A8 A0A024R7A8 P07943 P15121 P15121 P15122 P16116 P45376 P45376 P80276
(2 more...)
17-beta-estradiol 17-dehydrogenase. [EC: 1.1.1.62]
17-beta-estradiol + NAD(P)(+) = estrone + NAD(P)H.
  • The enzyme oxidizes or reduces the hydroxy/keto group on C(17) of estrogens and androgens in mammals and regulates the biological potency of these steroids.
  • The mammalian enzyme is bifunctional and also catalyzes EC 1.1.1.270.
  • The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, it is Si-specific with respect to NAD(P)(+).
 1 C9JRZ8