A4IL26 · A4IL26_GEOTN
- ProteinCopper-containing nitrite reductase
- GenenirK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids352 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
Catalytic activity
- Fe(III)-[cytochrome c] + H2O + nitric oxide = Fe(II)-[cytochrome c] + 2 H+ + nitrite
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 50 | Cu2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 68 | Cu2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 69 | Cu2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 71 | Cu2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 84 | Cu2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 107 | Cu2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 112 | Cu2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 124 | Cu2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 124 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 127 | Cu2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 127 | Cu2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 129 | Cu2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 129 | Cu2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 129 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 132 | Cu2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 163 | Cu2+ 10 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 163 | Cu2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 163 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 164 | Cu2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 164 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: C | ||||||
Binding site | 172 | Cu2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 172 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 177 | Cu2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 177 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: M | ||||||
Binding site | 196 | Cu2+ 12 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 198 | Cu2+ 13 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 211 | Cu2+ 14 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 255 | Cu2+ 15 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 268 | Cu2+ 16 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 268 | Cu2+ 17 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 273 | Cu2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 277 | Cu2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 278 | Cu2+ 11 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 280 | Cu2+ 18 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 291 | Cu2+ 19 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 299 | Cu2+ 20 (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 323 | Cu2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 323 | Cu cation 1 (UniProtKB | ChEBI); type 1 copper site | ||||
Sequence: H | ||||||
Binding site | 327 | Cu2+ 17 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | copper ion binding | |
Molecular Function | nitrite reductase (NO-forming) activity |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCopper-containing nitrite reductase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Geobacillus
Accessions
- Primary accessionA4IL26
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MNRNVYAVLSTVLAASLLA | ||||||
Chain | PRO_5039535300 | 20-352 | Copper-containing nitrite reductase | |||
Sequence: ACNSGGEQVKAESKNKTAATQQSEPNVIAAHKGVNQAPVPLKMERVGPHDVHIEMTAQITDIEIDKGKIYKAWTFNGQAPGPLVVVNEGDTIHFTLKNMDPVVPHSMDFHAVHASPSKDFIDVMPNKSGTFTYPANKPGVFMYHCGTKPVLQHIANGMHGVIIVKPKNGYPTDKEVDREYVLIQNEWYKYNDMNDFQNGVPSYVVFSSKALKPGDPNTNGDTFTLKEKPLLAKVGEKIRLYINNVGPNEVSSFHVVGTVFDDVYLDGNPNNHLQGMQTVMLPASGGAVVEFTVTRPGTYPIVTHQFNHAQKGAVAMLKVTETGEDDGTETSGH |
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 78-187 | Plastocyanin-like | ||||
Sequence: ITDIEIDKGKIYKAWTFNGQAPGPLVVVNEGDTIHFTLKNMDPVVPHSMDFHAVHASPSKDFIDVMPNKSGTFTYPANKPGVFMYHCGTKPVLQHIANGMHGVIIVKPKN | ||||||
Domain | 225-339 | Plastocyanin-like | ||||
Sequence: FSSKALKPGDPNTNGDTFTLKEKPLLAKVGEKIRLYINNVGPNEVSSFHVVGTVFDDVYLDGNPNNHLQGMQTVMLPASGGAVVEFTVTRPGTYPIVTHQFNHAQKGAVAMLKVT |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length352
- Mass (Da)38,382
- Last updated2007-05-01 v1
- Checksum5C243800B5B14094
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000557 EMBL· GenBank· DDBJ | ABO66030.1 EMBL· GenBank· DDBJ | Genomic DNA |