Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | uncultured bacterium |
Crystallization (Comment) | Organism |
---|---|
homology modeling based on PDB entry 1BKW. Model demonstrates that the enzyme can be folded into two cupredoxin domains of the well-known CuNIR structure and implies that the conserved residues H122, D125, H127, H158, C159, H168, M173,H272, and H321 form the type 1 and type 2 Cu sites | uncultured bacterium |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.25 | - |
nitrite | pH 6.5, 25°C | uncultured bacterium |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
copper | copper atoms are coordinated by H122, C159, H168, and M173 for the type 1 Cu site and H127, H158, and H321 for the type 2 Cu site. The absorption spectrum of NirK displays two peaks at 598 and 449 nm characteristic for type I Cu proteins | uncultured bacterium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
uncultured bacterium | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrite + reduced benzyl viologen | - |
uncultured bacterium | nitric oxide + oxidized benzyl viologen | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NirK | - |
uncultured bacterium |