PROSITE documentation PDOC00543
GMC oxidoreductases signatures


The following FAD flavoproteins oxidoreductases have been found [1,2] to be evolutionary related. These enzymes, which are called 'GMC oxidoreductases', are listed below.

  • Glucose oxidase (EC (GOX) from Aspergillus niger. Reaction catalyzed: glucose + oxygen -> delta-gluconolactone + hydrogen peroxide.
  • Methanol oxidase (EC (MOX) from fungi. Reaction catalyzed: methanol + oxygen -> acetaldehyde + hydrogen peroxide.
  • Choline dehydrogenase (EC (CHD) from bacteria. Reaction catalyzed: choline + acceptor -> βine acetaldehyde + reduced acceptor.
  • Glucose dehydrogenase (GLD) (EC from Drosophila. Reaction catalyzed: glucose + acceptor -> delta-gluconolactone + reduced acceptor.
  • L-sorbose 1-dehydrogenase (EC (SDH) from Gluconobacter oxydans. Reaction catylzed: L-sorbose + acceptor = 1-dehydro-L-sorbose + reduced acceptor.
  • Cholesterol oxidase (CHOD) (EC from Brevibacterium sterolicum and Streptomyces strain SA-COO. Reaction catalyzed: cholesterol + oxygen -> cholest-4-en-3-one + hydrogen peroxide.
  • AlkJ [3], an alcohol dehydrogenase from Pseudomonas oleovorans, which converts aliphatic medium-chain-length alcohols into aldehydes.
  • Cellobiose dehydrogenase (CDH) (EC from Phanerochaete chrysosporium.

This family also includes a lyase:

  • (R)-mandelonitrile lyase (EC (hydroxynitrile lyase) from plants [4], an enzyme involved in cyanogenis, the release of hydrogen cyanide from injured tissues.

These enzymes are proteins of size ranging from 556 (CHD) to 664 (MOX) amino acid residues which share a number of regions of sequence similarities. One of these regions, located in the N-terminal section, corresponds to the FAD ADP-binding domain. The function of the other conserved domains is not yet known; we have selected two of these domains as signature patterns. The first one is located in the N-terminal section of these enzymes, about 50 residues after the ADP-binding domain, while the second one is located in the central section.

Last update:

May 2008 / Text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

GMC_OXRED_1, PS00623; GMC oxidoreductases signature 1  (PATTERN)

GMC_OXRED_2, PS00624; GMC oxidoreductases signature 2  (PATTERN)


1AuthorsCavener D.R.
TitleGMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities.
SourceJ. Mol. Biol. 223:811-814(1992).
PubMed ID1542121

2AuthorsHenikoff S. Henikoff J.G.
TitleProtein family classification based on searching a database of blocks.
SourceGenomics 19:97-107(1994).
PubMed ID8188249

3Authorsvan Beilen J.B. Eggink G. Enequist H. Bos R. Witholt B.
SourceMol. Microbiol. 6:3121-3136(1992).

4AuthorsCheng I.P. Poulton J.E.
SourcePlant Cell Physiol. 34:1139-1143(1993).

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)