Reviewed,
UniProtKB/Swiss-Prot A6L890 (NRFA_PARD8)
Last modified
June 16, 2009.
Version 17.
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 | Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / NCTC 11152) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 435591 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Porphyromonadaceae › Parabacteroides |
Protein attributes
| Sequence length | 494 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 | Repeat 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 iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW 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 – 31 | 31 | Potential | ||||||
| Chain | 32 – 494 | 463 | Cytochrome c-552 HAMAP MF_01182 | PRO_1000065804 | |||||
Sites | |||||||||
| Metal binding | 116 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 148 | 1 | Iron (heme 1 axial ligand) By similarity | ||||||
| Metal binding | 186 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 228 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 230 | 1 | Calcium By similarity | ||||||
| Metal binding | 231 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 276 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 278 | 1 | Calcium By similarity | ||||||
| Metal binding | 290 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 301 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Metal binding | 315 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 332 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 407 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Binding site | 144 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 147 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 182 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 185 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 224 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 227 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 231 | 1 | Substrate By similarity | ||||||
| Binding site | 279 | 1 | Substrate By similarity | ||||||
| Binding site | 297 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 300 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 328 | 1 | Heme 5 (covalent) By similarity | ||||||
| Binding site | 331 | 1 | Heme 5 (covalent) By similarity | ||||||
Sequences
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References
| [1] | "Evolution of symbiotic bacteria in the distal human intestine." Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I. PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000140 Genomic DNA. Translation: ABR41904.1. | |
| RefSeq | YP_001301526.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5305200. |
| GenomeReviews | Gene locus BDI_0109 in contig CP000140_GR. |
| KEGG | pdi:BDI_0109. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A6L890. HKESGAP. |
Family and domain databases | |
| HAMAP | MF_01182. [Tree] |
| InterPro | IPR003321. Cyt_c552. IPR011031. Multihaem_cyt. [Graphical view] |
| Pfam | PF02335. Cytochrom_C552. 1 hit. [Graphical view] |
| PIRSF | PIRSF000243. Cyt_c552. 1 hit. |
| PROSITE | PS51008. MULTIHEME_CYTC. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NRFA_PARD8 | ||||||||
| Accession | Primary (citable) accession number: A6L890 | ||||||||
| 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


