Trimethylamine dehydrogenase/Dimethylamine dehydrogenase, FMN-binding domain (IPR037348)

Short name: TMADH/HD_FMN-bd

Overlapping homologous superfamilies

Domain relationships


This entry represents the FMN-binding domain found in trimethylamine dehydrogenase (TMADH) and histamine dehydrogenase (HD). TMADH is an iron-sulfur flavoprotein that catalyzes the oxidative demethylation of trimethylamine to form dimethylamine and formaldehyde. The protein forms a symetrical dimer with each subunit containing one 4Fe-4S cluster and one FMN cofactor [PMID: 3771568]. It contains a unique flavin, in the form of a 6-S-cysteinyl FMN which is bent by ~25 degrees along the N5-N10 axis of the flavin isoalloxazine ring. This modification of the conformation of the flavin is thought to facilitate catalysis [PMID: 2545689, PMID: 3771568, PMID: 15777008, PMID: 11192721, PMID: 16377910]. The closely related histamine dehydrogenase catalyzes oxidative deamination of histamine [PMID: 15311941].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0010181 FMN binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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