A0A0Q6GNV9 · A0A0Q6GNV9_9HYPH
- ProteinCopper-containing nitrite reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids378 (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 | 133 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 138 | Cu cation 2 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 173 | Cu cation 2 (UniProtKB | ChEBI); type 2 copper site | ||||
Sequence: H | ||||||
Binding site | 174 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 183 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 188 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M | ||||||
Binding site | 344 | Cu cation 2 (UniProtKB | ChEBI); type 2 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 > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium
Accessions
- Primary accessionA0A0Q6GNV9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-33 | |||||
Sequence: MSTTFPVTRRSILAGAAFAGALAPLVAASAANA | ||||||
Chain | PRO_5015214312 | 34-378 | Copper-containing nitrite reductase | |||
Sequence: SAEAVNVKAAPADLANLKRVKLELVNPPFVHPHSQTAEGDPRIYEVTLTIQEKKIVIDDAGTEVHAMTFNGSVPGPMIVVHQDDYVEITLVNPETNELQHNIDFHSATGALGGGALTAVNPGEKAVMRFKATKAGVFVYHCAPPGMVPWHVTSGMNGAIMVLPRDGLKDHKGNNLVYDRVYYVGEQDFYVPKGADGQYKTYESAGEAYGEVLEVMNTLIPSHIVFNGAVGALTGENALQAKVGEKVLILHSQANRDTRPHLIGGHGDYVWATGKFANAPELDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNLIEAFEKGAAAHFKVEGEWNNDLMTGIVSPNNH |
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 91-197 | Plastocyanin-like | ||||
Sequence: DDAGTEVHAMTFNGSVPGPMIVVHQDDYVEITLVNPETNELQHNIDFHSATGALGGGALTAVNPGEKAVMRFKATKAGVFVYHCAPPGMVPWHVTSGMNGAIMVLPR | ||||||
Domain | 214-364 | Plastocyanin-like | ||||
Sequence: YYVGEQDFYVPKGADGQYKTYESAGEAYGEVLEVMNTLIPSHIVFNGAVGALTGENALQAKVGEKVLILHSQANRDTRPHLIGGHGDYVWATGKFANAPELDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNLIEAFEKGAAAHFKVEGEW |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length378
- Mass (Da)40,484
- Last updated2016-01-20 v1
- Checksum454C97E055D7CC05
Keywords
- Technical term