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: waiting to be named.

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 17576: Acyl-CoA dehydrogenase family member 10

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
Kanamycin kinase. [EC: 2.7.1.95]
ATP + kanamycin = ADP + kanamycin 3'-phosphate.
  • Also acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A.
  • An enzyme from Pseudomonas aeruginosa also acts on butirosin.
24 A0A0K1EF61 A0A0K1EF61 A0A0X8R757 A0A0X8R757 A0A173KZH8 A0A173KZH8 G0ERH1 G0ERH1 G0F0B4 G0F0B4
(14 more...)
Medium-chain acyl-CoA dehydrogenase. [EC: 1.3.8.7]
A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
  • One of several enzymes that catalyze the first step in fatty acids beta-oxidation.
  • The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C(8) to C(12) compounds.
  • The enzyme from rat does not accept C(16) at all and is most active with C(6)-C(8) compounds.
  • cf. EC 1.3.8.1, EC 1.3.8.8 and EC 1.3.8.9.
  • Formerly EC 1.3.2.2 and EC 1.3.99.3.
6 A0A173L1F7 A0A173L1F7 U2E6G5 U2E6G5 U2FWT0 U2FWT0
Transferred entry: 1.3.8.7, 1.3.8.8 and 1.3.8.9. [EC: 1.3.99.3]
    2 A9HVQ1 A9HVQ1
    Thiamine phosphate synthase. [EC: 2.5.1.3]
    (1) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy- 4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (2) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-(2-carboxy-4- methylthiazol-5-yl)ethyl phosphate = diphosphate + thiamine phosphate + CO(2). (3) 4-amino-2-methyl-5-diphosphomethylpyrimidine + 4-methyl-5- (2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate.
    • The enzyme catalyzes the penultimate reaction in thiamine de novo biosynthesis, condensing the pyrimidine and thiazole components.
    • The enzyme is thought to accept the product of EC 2.8.1.10 as its substrate.
    • However, it has been shown that in some bacteria, such as Bacillus subtilis, an additional enzyme, EC 5.3.99.10 converts that compound into its tautomer 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate, and that it is the latter that serves as the substrate for the synthase.
    • In addition to this activity, the enzyme participates in a salvage pathway, acting on 4-methyl-5-(2-phosphono-oxyethyl)thiazole, which is produced from thiamine degradation products.
    • In yeast this activity is found in a bifunctional enzyme and in the plant Arabidopsis thaliana the activity is part of a trifunctional enzyme.
    2 A6FNB2 A6FNB2
    (R)-benzylsuccinyl-CoA dehydrogenase. [EC: 1.3.8.3]
    (R)-2-benzylsuccinyl-CoA + electron-transfer flavoprotein = (E)-2- benzylidenesuccinyl-CoA + reduced electron-transfer flavoprotein.
    • Unlike other acyl-CoA dehydrogenases, this enzyme exhibits high substrate- and enantiomer specificity it is highly specific for (R)- benzylsuccinyl-CoA and is inhibited by (S)-benzylsuccinyl-CoA.
    • Forms the third step in the anaerobic toluene metabolic pathway in Thauera aromatica.
    • Ferricenium ion is an effective artificial electron acceptor.
    • Formerly EC 1.3.99.21.
    2 A0A0M7HJD5 A0A0M7HJD5
    3-isopropylmalate dehydratase. [EC: 4.2.1.33]
    (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.
    • Forms part of the leucine-biosynthesis pathway.
    • Brings about the interconversion of the two isomers of isopropylmalate.
    2 U2WS27 U2WS27
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