A0A0Q8WMW5 · A0A0Q8WMW5_9BURK
- ProteinCopper-containing nitrite reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids360 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H+ + nitrite
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Cu+ ion.
Note: Binds 1 Cu+ ion.
Pathway
Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 113 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 118 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 153 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 154 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 163 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 168 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M | ||||||
Binding site | 324 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | copper ion binding | |
Molecular Function | nitrite reductase (NO-forming) activity | |
Biological Process | denitrification pathway | |
Biological Process | nitrate assimilation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCopper-containing nitrite reductase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Achromobacter
Accessions
- Primary accessionA0A0Q8WMW5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MNALRPTLLAAALVLTMAGGPAFA | ||||||
Chain | PRO_5015216007 | 25-360 | Copper-containing nitrite reductase | |||
Sequence: QNADKLPRAKVTLVAPPMVHPHEQVAKSGPKVIEFVMTIEEKKMVIDDKGTTLQAMTFNGSMPGPTMVVHEGDYVEVTLVNPASNAMPHNVDFHAATGALGGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMVLPREGLKDPQGKPLHYDRAYTIGEFDLYIPKDGNGKYKDYATLAESYGDTVEVMRKLTPSHIVFNGKVGALTGNNALTAKVGETVLLIHSQANRDTRPHLIGGHGDWVWETGKFGNPPEKNLETWFIRGGSAGAALYTFKQPGVYAYLNHNLIEAFELGAAGHIKVEGKWNDDLMKQIKAPGPIPR |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 69-178 | Plastocyanin-like | ||||
Sequence: VIDDKGTTLQAMTFNGSMPGPTMVVHEGDYVEVTLVNPASNAMPHNVDFHAATGALGGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMVLPRE | ||||||
Domain | 193-344 | Plastocyanin-like | ||||
Sequence: AYTIGEFDLYIPKDGNGKYKDYATLAESYGDTVEVMRKLTPSHIVFNGKVGALTGNNALTAKVGETVLLIHSQANRDTRPHLIGGHGDWVWETGKFGNPPEKNLETWFIRGGSAGAALYTFKQPGVYAYLNHNLIEAFELGAAGHIKVEGKW |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length360
- Mass (Da)38,929
- Last updated2016-01-20 v1
- ChecksumECA6675B24269B3B