J2UFR1 · J2UFR1_9PSED
- ProteinNitrous-oxide reductase
- GenenosZ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids639 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.
Catalytic activity
- N2 + 2 Fe(III)-[cytochrome c] + H2O = nitrous oxide + 2 Fe(II)-[cytochrome c] + 2 H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 calcium ions per subunit.
Note: Binds 6 Cu cations per subunit. Each subunit contains 2 copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site of nitrous oxide reduction.
Pathway
Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 130 | Cu cation Z2 (UniProtKB | ChEBI) | |||
Binding site | 131 | Cu cation Z3 (UniProtKB | ChEBI) | |||
Binding site | 179 | Cu cation Z2 (UniProtKB | ChEBI) | |||
Binding site | 257 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 260 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 268 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 274 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 325 | Ca2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 327 | Cu cation Z1 (UniProtKB | ChEBI) | |||
Binding site | 383 | Cu cation Z1 (UniProtKB | ChEBI) | |||
Binding site | 434 | Cu cation Z3 (UniProtKB | ChEBI) | |||
Binding site | 455 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 470 | Ca2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 495 | Cu cation Z4 (UniProtKB | ChEBI) | |||
Binding site | 584 | Cu cation A1 (UniProtKB | ChEBI) | |||
Binding site | 619 | Cu cation A1 (UniProtKB | ChEBI) | |||
Binding site | 619 | Cu cation A2 (UniProtKB | ChEBI) | |||
Binding site | 621 | Cu cation A2 (UniProtKB | ChEBI) | |||
Binding site | 623 | Cu cation A1 (UniProtKB | ChEBI) | |||
Binding site | 623 | Cu cation A2 (UniProtKB | ChEBI) | |||
Binding site | 627 | Cu cation A2 (UniProtKB | ChEBI) | |||
Binding site | 630 | Cu cation A1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | periplasmic space | |
Molecular Function | calcium ion binding | |
Molecular Function | copper ion binding | |
Molecular Function | cytochrome-c oxidase activity | |
Molecular Function | nitrous-oxide reductase activity | |
Biological Process | denitrification pathway |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNitrous-oxide reductase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionJ2UFR1
Proteomes
Subcellular Location
PTM/Processing
Post-translational modification
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-19 | Basic and acidic residues | |||
Region | 1-21 | Disordered | |||
Domain | 540-639 | Cytochrome oxidase subunit II copper A binding | |||
Region | 543-639 | COX2-like | |||
Sequence similarities
Belongs to the NosZ family.
In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length639
- Mass (Da)71,248
- Last updated2012-10-03 v1
- Checksum9DC185E2DD0619E8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-19 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AKJH01000023 EMBL· GenBank· DDBJ | EJM91426.1 EMBL· GenBank· DDBJ | Genomic DNA |