Glucose-methanol-choline oxidoreductase (IPR012132)

Short name: GMC_OxRdtase

Overlapping homologous superfamilies

Family relationships


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:, alcohol oxidase (EC:, glucose oxidase (EC:, choline dehydrogenase (EC:, 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].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0050660 flavin adenine dinucleotide binding
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.