| Type: | Domain | Name: | Ammonia/methane monooxygenase, subunit B, helix hairpin domain |
| Description: | Ammonia monooxygenase and the particulate methane monooxygenase are both integral membrane proteins, occurring in ammonia oxidisers and methanotrophs respectively, which are thought to be evolutionarily related []. These enzymes have a relatively wide substrate specificity and can catalyse the oxidation of a range of substrates including ammonia, methane, halogenated hydrocarbons and aromatic molecules []. These enzymes are composed of 3 subunits - A (), B () and C () - and contain various metal centres, including copper. Particulate methane monooxygenase from Methylococcus capsulatus str. Bathis an ABC homotrimer, which contains mononuclear and dinuclear copper metal centres, and a third metal centre containing a metal ion whose identity in vivo is not certain[].The soluble regions of these enzymes derive primarily from the B subunit. This subunit forms two antiparallel beta-barrel-like structures and contains the mono- and di- nuclear copper metal centres [].This entry represents the beta hairpin that links the two beta barrels. | Short Name: | NH3_CH4_mOase_suB_hlx_hairpin |
