| UniProt functional annotation for P18798 | |||
| UniProt code: P18798. |
| Organism: | Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath). | |
| Taxonomy: | Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales; Methylococcaceae; Methylococcus. | |
| Function: | 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. | |
| Catalytic activity: | Reaction=H(+) + methane + NADH + O2 = H2O + methanol + NAD(+); Xref=Rhea:RHEA:13637, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.25; | |
| Catalytic activity: | Reaction=H(+) + methane + NADPH + O2 = H2O + methanol + NADP(+); Xref=Rhea:RHEA:13641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.25; | |
| Subunit: | M.capsulatus has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. | |
Annotations taken from UniProtKB at the EBI.