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:

"
SCP2 sterol-binding 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 2040: Non-specific lipid-transfer protein-like 1

There are 6 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
Propanoyl-CoA C-acyltransferase. [EC: 2.3.1.176]
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-trihydroxy-24-oxo-5-beta-cholestanoyl- CoA.
  • Also acts on dihydroxy-5-beta-cholestanoyl-CoA and other branched chain acyl-CoA derivatives.
  • Catalyzes the penultimate step in the formation of bile acids.
  • The bile acid moiety is transferred from the acyl-CoA thioester (RCO- SCoA) to either glycine or taurine (NH(2)R') by EC 2.3.1.65.
  • Formerly EC 2.3.1.154.
13 A0A0B2PYI2 A0A0B2RV47 B7PKM5 C6T0J9 C6T1B1 E0VAE7 G0R1L1 O62742 P07857 P11915
(3 more...)
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase. [EC: 4.2.1.107]
(24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestanoyl- CoA = (24E)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl- CoA + H(2)O.
  • Forms part of the rat peroxisomal multifunctional enzyme perMFE-2, which also exhibits a dehydrogenase activity.
  • Involved in the beta-oxidation of the cholesterol side chain in the cholic-acid biosynthesis pathway.
2 B7PLL8 E0VSA3
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)(+).
2 A3LP20 Q9VY92
L-xylulose reductase. [EC: 1.1.1.10]
Xylitol + NADP(+) = L-xylulose + NADPH.
    1 B7PKM5
    3-hydroxyacyl-CoA dehydrogenase. [EC: 1.1.1.35]
    (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
    • Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate.
    • Some enzymes act, more slowly, with NADP(+).
    • Broad specificity to acyl chain-length (cf. EC 1.1.1.211).
    1 Q9NKW1
    Glucose 1-dehydrogenase (NAD(P)(+)). [EC: 1.1.1.47]
    D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H.
    • This enzyme has similar activity with either NAD(+) or NADP(+).
    • Cf. EC 1.1.1.118 and EC 1.1.1.119.
    1 E0VM98