EC Number   |
General Information |
Reference |
|---|
    1.14.99.39 | evolution |
nitrifying bacteria are responsible for ammonia oxidation and mainly belong to the Proteobacteria or Nitrospira phyla, comparison of bacterial community profiles among DNA libraries rom analyzed in Proteobacteria from composts produced from either food waste or cattle manure |
745410 |
| 1.14.99.39 | evolution |
particulate methane monooxygenase and ammonia monooxygenase are evolutionarily related enzymes despite their different physiological roles in these bacteria. Nitrosococcus oceonus AmoA shows higher identity to PmoA (methane monooxygenase) sequences from other members of the gamma-proteobacteria than to AmoA sequences |
697966 |
| 1.14.99.39 | evolution |
phylogenetic diversity of archaea and the archaeal ammonia monooxygenase gene in populations from uranium mining-impacted locations in Bulgaria, phylogenetic analysis. The main pollutants were Cu and Zn, U, Cr, As, Pb, and sulfates, dependent on the location, overview |
744185 |
| 1.14.99.39 | evolution |
reconstruction of AmoA protein sequence evolution during a major evolutionary transition to acidophily in the C14 lineage of Nitrosotalea, and ancestral reconstruction of sequence changes fixed in the AmoA protein during the evolutionary transition to acidophily in the C11 lineage of Nitrososphaera, AmoA protein evolution during ancestral pH adaptation events, nature of selection associated with AmoA evolution, overview. Three pH-adapted lineages are particularly important in terms of their high abundance in contemporary terrestrial ecosystems, i.e. the phylogenetically-distant acidophilic lineages called C11 (within Nitrososphaera) and C14/C15 (within Nitrosotalea) and the alkalinophilic lineage called C1/2 (within Nitrososphaera) |
745775 |
| 1.14.99.39 | evolution |
the enzyme belongs to the ammonia monooxygenase (AMO)/particulate methane monooxygenase (pMMO) superfamily, copper membrane-associated monooxygenases (CuMOs), which is a diverse group of membrane-bound enzymes. The Ny_amoB structure reveals that the fold of the N-terminal domain of the B subunit in the AMO/pMMO superfamily is very well conserved as is the presence of an N-terminal copper binding site |
746404 |
| 1.14.99.39 | malfunction |
two copies of amoA (amoA1 and amoA2), they differ by one nucleotide. Either copy of amoA is sufficient to support growth when the other copy is disrupted. Inactivation of amoA1 results in slower growth |
698553 |
| 1.14.99.39 | malfunction |
two copies of amoA (amoA1 and amoA2), they differ by one nucleotide. Either copy of amoA is sufficient to support growth when the other copy is disrupted. Inactivation of amoA2 does not results in slower growth |
698553 |
| 1.14.99.39 | metabolism |
nitrification is a fundamental process in the marine nitrogen cycle that makes fixed nitrogen available in the form of nitrite and nitrate to primary producers and for denitrification and anaerobic ammonium oxidation. Nitrification results from the combination of two processes: ammonia oxidation and nitrite oxidation. The ammonia oxidation process starts with the oxidation of ammonia to hydroxylamine, which is catalyzed by ammonia monoxygenase, AMO |
716123 |
| 1.14.99.39 | metabolism |
Nitrosomonas europaea is an aerobic nitrifying bacterium that oxidizes ammonia (NH3) to nitrite (NO2-) through the sequential activities of ammonia monooxygenase (AMO) and hydroxylamine dehydrogenase (HAO) |
-, 744103 |
| 1.14.99.39 | more |
AmoC subunit confers greater enzyme stability. Enzyme expression in stress response, overview |
727758 |
