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Methanol oxidation system protein MoxJ; the type 2 periplasmic binding fold. This predicted periplasmic protein, called MoxJ or MxaJ, is required for methanol oxidation in Methylobacterium extorquens. Homology suggests it is the substrate-binding protein of an ABC transporter associated with methanol oxidation. Other evidence also suggests that MoxJ is an accessory factor or additional subunit of methanol dehydrogenase itself. Mutational studies show a dependence on this protein for expression of the PQQ-dependent, two-subunit methanol dehydrogenase (MxaF and MxaI) in Methylobacterium extorquens, as if it is a chaperone for enzyme assembly or a third subunit. A homologous N-terminal sequence was found in Paracoccus denitrificans as a 32Kd third subunit. MoxJ may be both, a component of a periplasmic enzyme that converts methanol to formaldehyde and a component of an ABC transporter that delivers the resulting formaldehyde to the cell's interior. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",