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UniProt functional annotation for Q53239 | ||
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| UniProt code: Q53239. |
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| Organism: | |
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3). |
| Taxonomy: | |
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Luteovulum. |
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| Catalytic activity: | |
Reaction=[Fe(III)cytochrome c] + H2O + nitric oxide = [Fe(II)cytochrome c] + 2 H(+) + nitrite; Xref=Rhea:RHEA:15233, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.7.2.1; |
| Cofactor: | |
Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250}; Note=Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues from each of 2 monomers of the trimer. Nitrite is bound to the Cu(2+) ion site. Pseudoazurin is the physiological electron donor for the Cu-NIR in vitro. {ECO:0000250}; |
| Cofactor: | |
Name=Cu(+); Xref=ChEBI:CHEBI:49552; Evidence={ECO:0000250}; Note=Binds 1 Cu(+) ion. The Cu(+) ion is bound within a single monomer. {ECO:0000250}; |
| Cofactor: | |
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; |
| Pathway: | |
Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4. |
| Subunit: | |
Homotrimer. {ECO:0000250}. |
| Subcellular location: | |
Periplasm {ECO:0000250}. |
| Domain: | |
The type I copper site in NIR plays a crucial role for electron transfer from pseudoazurin to the type II copper site of NIR, which comprises the catalytic center of NIR for the reduction of nitrite. |
| Ptm: | |
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. |
| Similarity: | |
Belongs to the multicopper oxidase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.