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CATH Superfamily 2.140.10.10

Quinoprotein alcohol dehydrogenase-like superfamily

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
Quinoprotein alcohol dehydrogenase-like superfamily
".

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 3: Methanol dehydrogenase, large subunit

There are 3 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
Alcohol dehydrogenase (cytochrome c). [EC: 1.1.2.8]
A primary alcohol + 2 cytochrome c = an aldehyde + 2 reduced cytochrome c + 2 H(+).
  • A periplasmic PQQ-containing quinoprotein.
  • Occurs in Pseudomonas and Rhodopseudomonas.
  • The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c(550) as electron acceptor.
  • Acts on a wide range of primary and secondary alcohols, but not methanol.
  • It has a homodimeric structure (contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)).
  • It is routinely assayed with phenazine methosulfate as electron acceptor.
  • Activity is stimulated by ammonia or amines.
  • Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
  • Formerly EC 1.1.99.8.
 36 A0A072ZDU0 A0A072ZDU0 A0A072ZDU0 A0A072ZDU0 A0A072ZDU0 A0A072ZDU0 A0A1G5LYL3 A0A1G5LYL3 A0A1G5LYL3 A0A1G5LYL3
(26 more...)
Alcohol dehydrogenase (azurin). [EC: 1.1.9.1]
A primary alcohol + azurin = an aldehyde + reduced azurin.
  • Occurs in Comamonas and Pseudomonas.
  • Does not require an amine activator.
  • Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate.
  • Usually assayed with phenazine methosulfate or ferricyanide.
  • Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
  • Formerly EC 1.1.98.1.
 10 A0A1Y3KLH3 A0A1Y3KLH3 A0A1Y3KLH3 A0A2S6W5X4 A0A2S6W5X4 A0A2S6W5X4 Q4W6G0 Q8GR64 Q8GR64 Q8GR64
Lupanine 17-hydroxylase (cytochrome c). [EC: 1.17.2.2]
Lupanine + 2 ferricytochrome c + H(2)O = 17-hydroxylupanine + 2 ferrocytochrome c + 2 H(+).
    		 1 Q934G0
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