Q9HYL2 · NOSZ_PSEAE
- ProteinNitrous-oxide reductase
- GenenosZ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids636 (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 | 127 | Cu cation Z2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | Cu cation Z3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 176 | Cu cation Z2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 254 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 257 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 265 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 271 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 322 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 324 | Cu cation Z1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 380 | Cu cation Z1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 431 | Cu cation Z3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 452 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 467 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 492 | Cu cation Z4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 581 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 616 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 616 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 618 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 620 | Cu cation A1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 620 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 624 | Cu cation A2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 627 | 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 > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9HYL2
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-49 | Tat-type signal | ||||
Sequence: MSDDTKSPHEETHGLNRRGFLGASALTGAAALVGASALGSAVVGREARA | ||||||
Chain | PRO_0000019828 | 50-636 | Nitrous-oxide reductase | |||
Sequence: AGKGERSKAEVAPGELDEYYGFWSGGHSGEVRVLGVPSMRELMRIPVFNVDSATGWGLTNESKRVLGDSARFLNGDCHHPHISMTDGKYDGKYLFINDKANSRVARIRLDVMKCDRIVTIPNVQAIHGLRLQKVPHTRYVFCNAEFIIPHPNDGSTFDLSGDNAFTLYNAIDAETMEVAWQVIVDGNLDNTDMDYSGRFAASTCYNSEKAVDLGGMMRNERDWVVVFDIPRIEAEIKAKRFVTLGDSKVPVVDGRRKDGKDSPVTRYIPVPKNPHGLNTSPDGKYFIANGKLSPTCTMIAIERLGDLFAGKLADPRDVVVGEPELGLGPLHTTFDGRGNAYTTLFIDSQLVKWNLADAVRAYKGEKVDYIRQKLDVQYQPGHNHATLCETSEADGKWIVVLSKFSKDRFLPTGPLHPENDQLIDISGEEMKLVHDGPTFAEPHDCILARRDQIKTRKIWDRKDPFFAETVKRAEKDGIDLMKDNKVIREGNKVRVYMVSMAPSFGLTEFKVKQGDEVTVTITNLDEIEDVTHGFVMVNHGVCMEISPQQTSSITFVADKPGVHWYYCSWFCHALHMEMCGRMLVEKA |
Post-translational modification
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 302-322 | Disordered | ||||
Sequence: DGRRKDGKDSPVTRYIPVPKN | ||||||
Region | 540-636 | COX2-like | ||||
Sequence: NKVRVYMVSMAPSFGLTEFKVKQGDEVTVTITNLDEIEDVTHGFVMVNHGVCMEISPQQTSSITFVADKPGVHWYYCSWFCHALHMEMCGRMLVEKA |
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
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length636
- Mass (Da)70,660
- Last updated2001-01-11 v1
- ChecksumF3D66D519CF220BF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004091 EMBL· GenBank· DDBJ | AAG06780.1 EMBL· GenBank· DDBJ | Genomic DNA |