Biological Nitrogen Removal Database
A manually curated data resource for microbial nitrogen removal
Biological Nitrogen Removal Database
A manually curated data resource for microbial nitrogen removal
| Enzyme Name | Gene Culster | Enzyme Commission number | KEGG Orthology ID |
|
link |
|---|---|---|---|---|---|
| Ammonia monooxygenase (AMO) | amoA amoB amoC |
1.14.99.39 | K20934 K20933 K20932 | Ammonia monooxygenase (AMO) catalyzes the oxidation of ammonia to hydroxylamine, the first reaction in the process of ammonia oxidation to nitrite. | Link |
| Hydroxylamine oxidoreductase | haoA haoB |
1.7.2.6 | K10535 | The enzyme catalyzes the oxidation of hydroxylamine to nitrite via an enzyme-bound nitroxyl intermediate. The main product is nitrite, in some cases nitric oxide is produced as well. | Link |
| Nitrite oxidoreductase | nxrA nxrB nxrC nxD |
1.7.5.1 1.7.99.1 | K00370 K00371 | The enzyme catalyzes the oxidation of nitrite to nitrate via an enzyme-bound nitroxyl intermediate. Under unaerobic
conditions the enzyme is a nitrate reductase, catalyzing the reverse reaction. All known NOB oxidize nitrite by the enzyme NXR, which belongs to the type II group in the dimethyl sulfoxide reductase family of molybdopterin-cofactor-binding enzymes (Meincke et al., 1992; Lücker et al., 2010). NXR is membrane associated and contains an α subunit (NxrA) with the catalytic site and a β subunit (NxrB) that channels electrons derived from nitrite to downstream components of the respiratory chain (Kirstein and Bock, 1993). Most likely, a γ subunit (NxrC) functions as a membrane anchor that may be involved in electron transport (Lücker et al., 2010). |
Link |