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Dimethylamine monooxygenase subunit DmmA-like, N-terminal domain
This entry represents the N-terminal domain of the dimethylamine monooxygenase subunit DmmA from Methylocella silvestris (Msil_3607, Swiss:B8EJ00) and similar sequences, mainly found in proteobacteria and actinomycetes. Dimethylamine (DMA) monooxygenase is required for metabolism of trimethylamine N-oxide (TMAO) [1,2]. This domain may adopt a Rossmann-like fold similar to Ferredoxin/Ferric reductase-like NAD binding domain. [1]. 25088783. Identification and characterization of trimethylamine N-oxide (TMAO) demethylase and TMAO permease in Methylocella silvestris BL2. Zhu Y, Jameson E, Parslow RA, Lidbury I, Fu T, Dafforn TR, Schafer H, Chen Y;. Environ Microbiol. 2014;16:3318-3330. [2]. 28304370. Identification of dimethylamine monooxygenase in marine bacteria reveals a metabolic bottleneck in the methylated amine degradation pathway. Lidbury I, Mausz MA, Scanlan DJ, Chen Y;. ISME J. 2017;11:1592-1601. (from Pfam)
Ferric reductase NAD binding domain
FAD-binding oxidoreductase
Oxidoreductase NAD-binding domain
Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity. [1]. 1748631. The sequence of squash NADH:nitrate reductase and its relationship to the sequences of other flavoprotein oxidoreductases. A family of flavoprotein pyridine nucleotide cytochrome reductases. Hyde GE, Crawford NM, Campbell W;. J Biol Chem 1991;266:23542-23547. (from Pfam)
ferredoxin reductase
ferredoxin reductase, similar to stearoyl-CoA 9-desaturase electron transfer protein that is part of an acyl-CoA desaturase complex involved in the production of oleic acid
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