1.14.13.25	chcA, cytoplasmic methane monooxygenase, methane hydroxylase, methane mono-oxygenase, methane monooxygenase, methane monooxygenase hydroxylase, MmMmoC, MMO, MMO Bath, MMOB, MmoC, MMOH, MMOR, oxygenase, methane mono-, particulate methane monooxygenase, pMMO, sMMO, soluble methane monooxygenase, soluble methane monooxygenase hydroxylase	-	-, 438923, 438925, 438929, 438932, 438942, 438943, 438945, 438946, 438948, 438949, 658632, 671477, 671721, 671722, 672049, 672102, 672130, 672690, 673999, 674145, 674158, 674170, 675083, 675455, 676844, 684566, 685262, 685272, 701759, 701836, 703211, 703761, 704019, 704171, 704758, 706752, 711260, 712040, 712199, 726546, 728376, 744098, 744100, 744507, 744688, 744797, 744939, 745039, 745157, 745159, 745177, 745389, 745453, 745535, 745536, 745730, 746420, 764175, 764181, 764188, 764309, 764329, 764425, 764485, 764976, 764980, 765765	
1.14.13.25	MMOB	cofactor-free, monomeric component of sMMO, has regulatory role in catalysis	685272	
1.14.13.25	MMOH	diiron(II) center of the hydroxylase component of soluble methane monooxygenase	726546	
1.14.13.25	MMOH	hydroxylase component of sMMO, contains a binuclear nonheme iron active site that is essential for O2 activation and subsequent methane oxidation	685272	
1.14.13.25	sMMO	multicomponent enzyme	438950	
1.14.13.25	pMMO	particulate, membrane-bound enzyme form	-, 438943, 438945, 438946, 438947, 438948, 438949, 438950	
1.14.13.25	MMOR	reductase component of sMMO, contains a FAD cofactor and a [2Fe-2S] cluster, is responsible for transferring the reducing equivalents from NAD(P)H to MMOH	685272	
1.14.13.25	sMMO	soluble, cytoplasmic enzyme form	-, 438943, 438945, 438946, 438947, 438948, 438949, 438950	
1.14.13.25	sMMO	the enzyme contains three protein components, a 251 kDa hydroxylase (MMOH), a 38.6 kDa reductase (MMOR), and a 15.9 kDa regulatory protein (MMOB) required to couple electron consumption with substrate hydroxylation at the catalytic diiron center of MMOH	728376