Q65RI4 · NRFA_MANSM
- ProteinCytochrome c-552
- GenenrfA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids525 (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 | 129 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 157 | heme 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 160 | heme 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 161 | Fe (UniProtKB | ChEBI) of heme 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: K | ||||||
Binding site | 195 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 198 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 199 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 244 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 247 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 248 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 250 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 251 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 251 | substrate | ||||
Sequence: Y | ||||||
Binding site | 298 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 300 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 301 | substrate | ||||
Sequence: H | ||||||
Binding site | 312 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 319 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 322 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 323 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 338 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 353 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 356 | heme c 5 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 357 | Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 432 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Basfia
Accessions
- Primary accessionQ65RI4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MNGVIIVNILRKTLSSLAIVGLGFAMANSAVA | ||||||
Chain | PRO_0000268968 | 33-525 | Cytochrome c-552 | |||
Sequence: EEKAMATHQQAQQLQQPAPETAAKRAPTKEELTPVNPNLKIEAANEKFAADFPRQYNSWAKTAEQTEFHKEVEDDPRMIVMWGGYAFAKEFNSPRGHIYAVTDVRNILRTGSPKDANGGPQPMACWTCKGPDVPRLIAEWGEEGYFSGKWAKGGAEVVNSIGCADCHDTQSQDFKDGKPALRVARPHVLRALDTVGKTFATSDRTDQRAGVCANCHVEYYFDKSTGANNVVFPWYKGRDVDSIEKYYDEIGFKDWEHSISKAPMLKAQHPDFETWSMGTHGKNGVTCVDCHMAKTQDKDGKVYTDHQVVGNPVKDNFQNTCARCHDQSQDTLIKTVEQHKADVREVMLKLEDQLVKSHFEAKTAWDNGATQEEMKDALQAIRHAQWRWDFAAASHGMHMHAPDVALKIIASGLDRVADARAKLAVILAKHGVQQPIQYPDISTAEKAWKVMGIDIEKERKEKEEFIKTVIPEWNKEAISKGLILTAPPTTPAK |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 43-63 | Disordered | ||||
Sequence: AQQLQQPAPETAAKRAPTKEE |
Sequence similarities
Belongs to the cytochrome c-552 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length525
- Mass (Da)58,466
- Last updated2004-10-25 v1
- Checksum747EF08AFB3036BB
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016827 EMBL· GenBank· DDBJ | AAU38426.1 EMBL· GenBank· DDBJ | Genomic DNA |