Methane monooxygenase, D subunit.

Methane monooxygenase, A subunit, beta chain; Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.

Methane monooxygenase, B subunit; The B protein acts as a regulator of electron flow through the soluble mmo complex, switching the enzyme from an oxidase to a hydroxylase in the presence of the substrate; Belongs to the TmoD/XamoD family.

Methane monooxygenase, A subunit, gamma chain; Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.

Methane monooxygenase, B subunit; Methane monooxygenase is responsible for the initial oxygenation of methane to methanol in methanotrophs. At least in vitro, specific quinols can replace NADH as reductants.

Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Methane monooxygenase, C subunit; Identified by similarity to GP:14456716; match to protein family HMM PF04896.

Putative methanol dehydrogenase protein, large subunit; Identified by similarity to SP:P15279; match to protein family HMM PF01011.

NADH dehydrogenase I, C/D subunits; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family.