Reviewed,
UniProtKB/Swiss-Prot P45017 (NRFA_HAEIN)
Last modified
June 16, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
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 influenzae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 727 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 538 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 – 55 | 55 | Potential | ||||||
| Chain | 56 – 538 | 483 | Cytochrome c-552 HAMAP MF_01182 | PRO_0000006579 | |||||
Sites | |||||||||
| Metal binding | 133 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 165 | 1 | Iron (heme 1 axial ligand) By similarity | ||||||
| Metal binding | 203 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 268 | 1 | Iron (heme 3 axial ligand) By similarity | ||||||
| Metal binding | 270 | 1 | Calcium By similarity | ||||||
| Metal binding | 271 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 316 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 318 | 1 | Calcium By similarity | ||||||
| Metal binding | 330 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 341 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Metal binding | 356 | 1 | Iron (heme 2 axial ligand) By similarity | ||||||
| Metal binding | 373 | 1 | Iron (heme 5 axial ligand) By similarity | ||||||
| Metal binding | 448 | 1 | Iron (heme 4 axial ligand) By similarity | ||||||
| Binding site | 161 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 164 | 1 | Heme 1 (covalent) By similarity | ||||||
| Binding site | 199 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 202 | 1 | Heme 2 (covalent) By similarity | ||||||
| Binding site | 264 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 267 | 1 | Heme 3 (covalent) By similarity | ||||||
| Binding site | 271 | 1 | Substrate By similarity | ||||||
| Binding site | 319 | 1 | Substrate By similarity | ||||||
| Binding site | 337 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 340 | 1 | Heme 4 (covalent) By similarity | ||||||
| Binding site | 369 | 1 | Heme 5 (covalent) By similarity | ||||||
| Binding site | 372 | 1 | Heme 5 (covalent) By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
Cross-references
Sequence databases | |
|---|---|
| L42023 Genomic DNA. Translation: AAC22727.1. | |
| PIR | C64181. |
| RefSeq | NP_439227.3. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GU6 based on UniProtKB P32050. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 950047. |
| GenomeReviews | Gene locus HI1069 in contig L42023_GR. |
| KEGG | hin:HI1069. |
| NMPDR | fig|71421.1.peg.1028. |
| TIGR | HI1069. |
Phylogenomic databases | |
| HOGENOM | P45017. |
| OMA | P45017. CHDQSKE. |
Enzyme and pathway databases | |
| BioCyc | HINF71421:HI_1069-MON. |
| BRENDA | 1.7.2.2. 109. |
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_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P45017 | ||||||||
| 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
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


