A0A4R9X2G4 · A0A4R9X2G4_9HYPH
- ProteinNitrous-oxide reductase
- GenenosZ
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids641 (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
- 2 Fe(III)-[cytochrome c] + H2O + N2 = 2 Fe(II)-[cytochrome c] + 2 H+ + nitrous oxide
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 | 138 | Cu cation Z2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 139 | Cu cation Z3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 187 | Cu cation Z2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 328 | Cu cation Z1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 383 | Cu cation Z1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 434 | Cu cation Z3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 495 | Cu cation Z4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 584 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 619 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 619 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 621 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 623 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 623 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 627 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 630 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: M |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Mesorhizobium
Accessions
- Primary accessionA0A4R9X2G4
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 domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 540-641 | Cytochrome oxidase subunit II copper A binding | ||||
Sequence: RDGNKVRVYMTSAAPAFGLESFTVKQGDEVTVYVTNIDEVEDLTHGFAIVNYGINMEVASQATASVTFTANRAGVYWYYCSWFCHAMHMEMQGRMFVEPQAA | ||||||
Region | 543-641 | COX2-like | ||||
Sequence: NKVRVYMTSAAPAFGLESFTVKQGDEVTVYVTNIDEVEDLTHGFAIVNYGINMEVASQATASVTFTANRAGVYWYYCSWFCHAMHMEMQGRMFVEPQAA |
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
- Length641
- Mass (Da)70,601
- Last updated2019-07-31 v1
- ChecksumF34703EA3D4611F8