A0A1G5ZW48 · A0A1G5ZW48_9HYPH
- ProteinCopper-containing nitrite reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids368 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- nitric oxide + Fe(III)-[cytochrome c] + H2O = Fe(II)-[cytochrome c] + nitrite + 2 H+
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 | 119 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 124 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 159 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 160 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 170 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 175 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M | ||||||
Binding site | 331 | 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 > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Mesorhizobium
Accessions
- Primary accessionA0A1G5ZW48
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MFTRREALFGAAIGAAAVAAMPAFS | ||||||
Chain | PRO_5015211355 | 26-368 | Copper-containing nitrite reductase | |||
Sequence: ATITQADIKALPREKIKLVAPPFVHPHDQVAKTGPKVVEFTMTIEEKPVVIDADGTKLNAMTYNGTIPGPLMVVHQDDYVELTLINPDTNSLAHNIDFHAATGALGGGGLTLINPGEQVTLRFKATRTGTFVYHCAPGGPMIPWHVVSGMNGAIMVLPRDGLRNDQGKPVKYDRIFYIGESDFYIPRDEKGNFKSYESAGDGYDDIVKVMRGLIPTHVVFNGKVGSLTGDNAMKAKVGETVLIVHSQANRDTRPHLIGGHGDYVWEQGKFANPPAKDLETWFIRGGSAGSALYTFLQPGIYAYVNHNLIEAVELGATAHFMVEGTWNDDLMTQVEAPKPIAVN |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 79-184 | Plastocyanin-like | ||||
Sequence: DGTKLNAMTYNGTIPGPLMVVHQDDYVELTLINPDTNSLAHNIDFHAATGALGGGGLTLINPGEQVTLRFKATRTGTFVYHCAPGGPMIPWHVVSGMNGAIMVLPR | ||||||
Domain | 201-350 | Plastocyanin-like | ||||
Sequence: FYIGESDFYIPRDEKGNFKSYESAGDGYDDIVKVMRGLIPTHVVFNGKVGSLTGDNAMKAKVGETVLIVHSQANRDTRPHLIGGHGDYVWEQGKFANPPAKDLETWFIRGGSAGSALYTFLQPGIYAYVNHNLIEAVELGATAHFMVEGT |
Sequence similarities
Belongs to the multicopper oxidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length368
- Mass (Da)39,841
- Last updated2017-11-22 v1
- ChecksumF2A619BFCF7C70F6