Glucose-methanol-choline oxidoreductase (IPR012132)
Short name: GMC_OxRdtase
Overlapping homologous superfamilies
- FAD/NAD(P)-binding domain superfamily (IPR036188)
- Glucose-methanol-choline oxidoreductase (IPR012132)
- Glucose-methanol-choline oxidoreductase, actinobacteria (IPR023978)
- Oxygen-dependent choline dehydrogenase (IPR011533)
- Protein Hothead (IPR031206)
Proteins in this entry are members of the glucose-methanol-choline oxidoreductase family of flavoenzymes [PMID: 1542121]. These enzymes catalyse diverse reaction and include glucose dehydrogenase (EC:220.127.116.11), alcohol oxidase (EC:18.104.22.168), glucose oxidase (EC:22.214.171.124), choline dehydrogenase (EC:126.96.36.199), hydroxynitrile lyase (EC:188.8.131.52) and cyclase atC from Aspergillus terreus which oxidizes terremutin to terreic acid, a quinone epoxide inhibitor of a tyrosine kinase [PMID: 25265334].
Structural studies indicate that these proteins are composed of an N-terminal FAD-binding domain, and a C-terminal substrate-binding domain [PMID: 10216293, PMID: 11566130, PMID: 10194345]. The FAD-binding domain forms the alpha-beta fold typical of dinucleotide binding proteins, while the substrate-binding domain consists of a beta sheet surrounded by alpha helices. The general topology of these proteins is conserved, though inserted structural elements occur in both choline dehydrogenase and alcohol dehydrogenase [PMID: 9523716].
- PIRSF000137 (Alcohol_oxidase)