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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 34043: NAD(P)H quinone oxidoreductase, PIG3 family

There are 4 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.
 194 A0A009IVA4 A0A009IVA4 A0A045ILL3 A0A045ILL3 A0A059MHD2 A0A059MHD2 A0A060DDF4 A0A060DDF4 A0A074T4D2 A0A074T4D2
(184 more...)
Beta-ketoacyl-[acyl-carrier-protein] synthase I. [EC: 2.3.1.41]
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
  • Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain.
  • Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids.
  • Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)).
  • The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.
 60 A0A045ILL3 A0A045ILL3 A0A089QW18 A0A089QW18 A0A0B7DA56 A0A0B7DA56 A0A0C7DUP7 A0A0C7DUP7 A0A0D6J1T6 A0A0D6J1T6
(50 more...)
2-haloacrylate reductase. [EC: 1.3.1.103]
(S)-2-chloropropanoate + NADP(+) = 2-chloroacrylate + NADPH.
  • The enzyme acts in the degradation pathway of unsaturated organohalogen compounds by the bacterium Burkholderia sp. WS.
 4 A0A143QHH7 A0A143QHH7 A0A161GIR3 A0A161GIR3
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.
 2 G8SE29 G8SE29