A0A6I0JJS2 · A0A6I0JJS2_BACUN
- ProteinCytochrome c-552
- GenenrfA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids494 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process.
Catalytic activity
- 6 Fe(III)-[cytochrome c] + 2 H2O + NH4+ = 6 Fe(II)-[cytochrome c] + 8 H+ + nitrite
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Ca2+ ion per monomer.
Note: Binds 5 heme c groups covalently per monomer.
Pathway
Nitrogen metabolism; nitrate reduction (assimilation).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 116 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 144 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 147 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 148 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: K | ||||||
Binding site | 182 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 185 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 186 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 224 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 227 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 228 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 230 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 231 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 231 | substrate | ||||
Sequence: Y | ||||||
Binding site | 276 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 278 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 279 | substrate | ||||
Sequence: H | ||||||
Binding site | 290 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 297 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 300 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 301 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 315 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 328 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 331 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 332 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 407 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | periplasmic space | |
Molecular Function | calcium ion binding | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | nitrite reductase (cytochrome, ammonia-forming) activity | |
Biological Process | nitrate assimilation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome c-552
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA0A6I0JJS2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 12-32 | Helical | ||||
Sequence: LLFGGSMVVVFVLGLCVSALM |
Keywords
- Cellular component
Structure
Sequence
- Sequence statusComplete
- Length494
- Mass (Da)56,158
- Last updated2020-08-12 v1
- Checksum3A4FB03BC07320B3