O54069 (COX1_RICPR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 97.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable cytochrome c oxidase subunit 1 EC=1.9.3.1 Alternative name(s): Cytochrome aa3 subunit 1 Cytochrome c oxidase polypeptide I | ||||||
| Gene names |
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| Organism | Rickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 272947 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group › ![]() |
Protein attributes
| Sequence length | 534 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B By similarity. |
| Catalytic activity | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the heme-copper respiratory oxidase family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 534 | 534 | Probable cytochrome c oxidase subunit 1 | PRO_0000183449 | |||||||
Regions | |||||||||||
| Transmembrane | 35 – 55 | 21 | Helical; Potential | ||||||||
| Transmembrane | 76 – 96 | 21 | Helical; Potential | ||||||||
| Transmembrane | 97 – 117 | 21 | Helical; Potential | ||||||||
| Transmembrane | 120 – 140 | 21 | Helical; Potential | ||||||||
| Transmembrane | 165 – 185 | 21 | Helical; Potential | ||||||||
| Transmembrane | 202 – 222 | 21 | Helical; Potential | ||||||||
| Transmembrane | 254 – 274 | 21 | Helical; Potential | ||||||||
| Transmembrane | 286 – 306 | 21 | Helical; Potential | ||||||||
| Transmembrane | 320 – 340 | 21 | Helical; Potential | ||||||||
| Transmembrane | 357 – 377 | 21 | Helical; Potential | ||||||||
| Transmembrane | 396 – 416 | 21 | Helical; Potential | ||||||||
| Transmembrane | 433 – 453 | 21 | Helical; Potential | ||||||||
| Transmembrane | 475 – 495 | 21 | Helical; Potential | ||||||||
Sites | |||||||||||
| Metal binding | 81 | 1 | Iron (heme A axial ligand) Probable | ||||||||
| Metal binding | 260 | 1 | Copper B Probable | ||||||||
| Metal binding | 264 | 1 | Copper B Probable | ||||||||
| Metal binding | 309 | 1 | Copper B Probable | ||||||||
| Metal binding | 310 | 1 | Copper B Probable | ||||||||
| Metal binding | 395 | 1 | Iron (heme A3 axial ligand) Probable | ||||||||
| Metal binding | 397 | 1 | Iron (heme A axial ligand) Probable | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 260 ↔ 264 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The bacterial origin of mitochondria inferred from a phylogenetic analysis of the cytochrome b and cytochrome c oxidase I genes." Sicheritz T., Kurland C.G., Andersson S.G.E. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Madrid E. |
| [2] | "The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y13855 Genomic DNA. Translation: CAA74167.1. AJ235271 Genomic DNA. Translation: CAA14862.1. |
| PIR | D71698. |
| RefSeq | NP_220786.1. NC_000963.1. |
3D structure databases | |
| ProteinModelPortal | O54069. |
| SMR | O54069. Positions 21-530. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272947.RP405. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAA14862; CAA14862; CAA14862. |
| GeneID | 883394. |
| KEGG | rpr:RP405. |
| PATRIC | 17901591. VBIRicPro72556_0418. |
Phylogenomic databases | |
| eggNOG | COG0843. |
| HOGENOM | HOG000085274. |
| KO | K02274. |
| OMA | FLIGGIM. |
| ProtClustDB | CLSK870907. |
Enzyme and pathway databases | |
| UniPathway | UPA00705. |
Family and domain databases | |
| Gene3D | 1.20.210.10. 1 hit. |
| InterPro | IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view] |
| PANTHER | PTHR10422. PTHR10422. 1 hit. |
| Pfam | PF00115. COX1. 1 hit. [Graphical view] |
| PRINTS | PR01165. CYCOXIDASEI. |
| SUPFAM | SSF81442. COX1. 1 hit. |
| TIGRFAMs | TIGR02891. CtaD_CoxA. 1 hit. |
| PROSITE | PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX1_RICPR | ||||||||
| Accession | Primary (citable) accession number: O54069 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia prowazekii Rickettsia prowazekii (strain Madrid E): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
