Reviewed,
UniProtKB/Swiss-Prot P0ABL0 (NRFA_ECO57)
Last modified
February 9, 2010.
Version 37.
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 |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 478 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. HAMAP MF_01182 |
| 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. HAMAP MF_01182 Binds 5 heme groups covalently per monomer By similarity. HAMAP MF_01182 |
| Pathway | Nitrogen metabolism; nitrate reduction (assimilation). HAMAP MF_01182 |
| Subcellular location | Periplasm By similarity HAMAP MF_01182. |
| 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 – 26 | 26 | By similarity | ||||||
| Chain | 27 – 478 | 452 | Cytochrome c-552 HAMAP MF_01182 | PRO_0000042809 | |||||
Sites | |||||||||
| Metal binding | 94 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 126 | 1 | Iron (heme 1 axial ligand) By similarity | ||||||
| Metal binding | 164 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 213 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 215 | 1 | Calcium By similarity | ||||||
| Metal binding | 216 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 261 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 263 | 1 | Calcium By similarity | ||||||
| Metal binding | 275 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 286 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Metal binding | 301 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 318 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 393 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Binding site | 122 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 125 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 160 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 163 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 209 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 212 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 216 | 1 | Substrate By similarity | ||||||
| Binding site | 264 | 1 | Substrate By similarity | ||||||
| Binding site | 282 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 285 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 314 | 1 | Heme 5 (covalent) By similarity | ||||||
| Binding site | 317 | 1 | Heme 5 (covalent) By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG59268.1. BA000007 Genomic DNA. Translation: BAB38475.1. |
| PIR | D91260. |
| RefSeq | NP_290703.1. NP_313079.1. |
3D structure databases | |
| SMR | P0ABL0. Positions 37-477. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P0ABL0. |
Genome annotation databases | |
| GeneID | 914290. 960054. |
| GenomeReviews | Gene locus Z5669 in contig AE005174_GR. Gene locus ECs5052 in contig BA000007_GR. |
| KEGG | ece:Z5669. ecs:ECs5052. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG488281. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS5052-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01182. Cytochrom_C552. [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_ECO57 | ||||||||
| Accession | Primary (citable) accession number: P0ABL0 Secondary accession number(s): P32050 | ||||||||
| 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


