Reviewed,
UniProtKB/Swiss-Prot Q87ND9 (NRFA_VIBPA)
Last modified
November 4, 2008.
Version 41.
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 | Vibrio parahaemolyticus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 670 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 475 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 | NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+). |
| Cofactor | Binds 1 calcium ion per monomer By similarity. Binds 5 heme groups covalently per monomer By similarity. |
| Pathway | |
| Subcellular location | PeriplasmBy 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: HAMAP |
| 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 – 29 | 29 | Potential | ||||||
| Chain | 30 – 475 | 446 | Cytochrome c-552 | PRO_0000268982 | |||||
Sites | |||||||||
| Metal binding | 92 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 124 | 1 | Iron (heme 1 axial ligand) By similarity | ||||||
| Metal binding | 162 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 211 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 213 | 1 | Calcium By similarity | ||||||
| Metal binding | 214 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 259 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 261 | 1 | Calcium By similarity | ||||||
| Metal binding | 273 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 284 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Metal binding | 299 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 316 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 391 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Binding site | 120 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 123 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 158 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 161 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 207 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 210 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 214 | 1 | Substrate By similarity | ||||||
| Binding site | 262 | 1 | Substrate By similarity | ||||||
| Binding site | 280 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 283 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 312 | 1 | Heme 5 (covalent) By similarity | ||||||
| Binding site | 315 | 1 | Heme 5 (covalent) By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae." Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T. Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RIMD 2210633 / Serotype O3:K6. |
Cross-references
Sequence databases | |
|---|---|
| BA000031 Genomic DNA. Translation: BAC60192.1. | |
| RefSeq | NP_798308.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GU6 based on UniProtKB P32050. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1189436. |
| GenomeReviews | Gene locus VP1929 in contig BA000031_GR. |
| KEGG | vpa:VP1929. |
| NMPDR | fig|223926.1.peg.1929. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q87ND9. |
Enzyme and pathway databases | |
| BioCyc | VPAR223926:VP1929-MON. |
Family and domain databases | |
| HAMAP | MF_01182. [Tree] |
| InterPro | IPR003321. Cyt_c552. IPR017570. Cytc_552_NO2Rdtase_formate-dep. 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_VIBPA | ||||||||
| Accession | Primary (citable) accession number: Q87ND9 | ||||||||
| Entry history |
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| 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


