Reviewed,
UniProtKB/Swiss-Prot Q7VNX8 (NRFA_HAEDU)
Last modified
June 16, 2009.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytochrome c-552 EC=1.7.2.2 Alternative name(s): Ammonia-forming cytochrome c nitrite reductase Short name=Cytochrome c nitrite reductase | ||||
| Gene names |
| ||||
| Organism | Haemophilus ducreyi [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 730 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 502 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Plays a role in nitrite reduction By similarity. |
| Catalytic activity | NH3 + 2 H2O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H+. HAMAP MF_01182 |
| Cofactor | Binds 1 calcium ion per monomer By similarity. Binds 5 heme groups covalently per monomer By similarity. |
| Pathway | Nitrogen metabolism; nitrate reduction (assimilation). HAMAP MF_01182 |
| Subcellular location | Periplasm By similarity. |
| Sequence similarities | Belongs to the cytochrome c-552 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Calcium Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW nitrogen compound metabolic processInferred from electronic annotation. Source: HAMAP transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme bindingInferred from electronic annotation. Source: InterPro nitrite reductase (cytochrome, ammonia-forming) activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||
| Chain | 26 – 502 | 477 | Cytochrome c-552 HAMAP MF_01182 | PRO_0000268966 | |||||
Sites | |||||||||
| Metal binding | 105 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 137 | 1 | Iron (heme 1 axial ligand) By similarity | ||||||
| Metal binding | 175 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 224 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 226 | 1 | Calcium By similarity | ||||||
| Metal binding | 227 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 271 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 273 | 1 | Calcium By similarity | ||||||
| Metal binding | 285 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 296 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Metal binding | 311 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 328 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 403 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Binding site | 133 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 136 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 171 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 174 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 220 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 223 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 227 | 1 | Substrate By similarity | ||||||
| Binding site | 274 | 1 | Substrate By similarity | ||||||
| Binding site | 292 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 295 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 324 | 1 | Heme 5 (covalent) By similarity | ||||||
| Binding site | 327 | 1 | Heme 5 (covalent) By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Haemophilus ducreyi." Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 35000HP / ATCC 700724. |
Cross-references
Sequence databases | |
|---|---|
| AE017143 Genomic DNA. Translation: AAP95319.1. Different initiation. | |
| RefSeq | NP_872930.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GU6 based on UniProtKB P32050. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1490348. |
| GenomeReviews | Gene locus HD_0344 in contig AE017143_GR. |
| KEGG | hdu:HD0344. |
| NMPDR | fig|233412.1.peg.295. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q7VNX8. |
Enzyme and pathway databases | |
| BioCyc | HDUC233412:HD_0344-MON. |
| BRENDA | 1.7.2.2. 265031. |
Family and domain databases | |
| HAMAP | MF_01182. [Tree] |
| InterPro | IPR003321. Cyt_c552. IPR017570. Cyt_c_NO2Rdtase_formate-dep. IPR011031. Multihaem_cyt. [Graphical view] |
| Pfam | PF02335. Cytochrom_C552. 1 hit. [Graphical view] |
| PIRSF | PIRSF000243. Cyt_c552. 1 hit. |
| TIGRFAMs | TIGR03152. cyto_c552_HCOOH. 1 hit. |
| PROSITE | PS51008. MULTIHEME_CYTC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NRFA_HAEDU | ||||||||
| Accession | Primary (citable) accession number: Q7VNX8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


