PROSITE documentation PDOC00543GMC 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 1.1.3.4) (GOX) from Aspergillus niger. Reaction catalyzed: glucose + oxygen -> delta-gluconolactone + hydrogen peroxide.
- Methanol oxidase (EC 1.1.3.13) (MOX) from fungi. Reaction catalyzed: methanol + oxygen -> acetaldehyde + hydrogen peroxide.
- Choline dehydrogenase (EC 1.1.99.1) (CHD) from bacteria. Reaction catalyzed: choline + acceptor -> βine acetaldehyde + reduced acceptor.
- Glucose dehydrogenase (GLD) (EC 1.1.99.10) from Drosophila. Reaction catalyzed: glucose + acceptor -> delta-gluconolactone + reduced acceptor.
- L-sorbose 1-dehydrogenase (EC 1.1.99.32) (SDH) from Gluconobacter oxydans. Reaction catylzed: L-sorbose + acceptor = 1-dehydro-L-sorbose + reduced acceptor.
- Cholesterol oxidase (CHOD) (EC 1.1.3.6) 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 1.1.98.18) from Phanerochaete chrysosporium.
This family also includes a lyase:
- (R)-mandelonitrile lyase (EC 4.1.2.10) (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.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Cavener D.R. |
| Title | GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities. | |
| Source | J. Mol. Biol. 223:811-814(1992). | |
| PubMed ID | 1542121 |
| 2 | Authors | Henikoff S. Henikoff J.G. |
| Title | Protein family classification based on searching a database of blocks. | |
| Source | Genomics 19:97-107(1994). | |
| PubMed ID | 8188249 |
| 3 | Authors | van Beilen J.B. Eggink G. Enequist H. Bos R. Witholt B. |
| Source | Mol. Microbiol. 6:3121-3136(1992). |
| 4 | Authors | Cheng I.P. Poulton J.E. |
| Source | Plant Cell Physiol. 34:1139-1143(1993). |
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