Q02766 (COX1_PLAFA) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 78.
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: Cytochrome c oxidase subunit 1 EC=1.9.3.1 Alternative name(s): Cytochrome c oxidase polypeptide I | ||||
| Gene names |
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| Encoded on | Mitochondrion | ||||
| Organism | Plasmodium falciparum | ||||
| Taxonomic identifier | 5833 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)![]() |
Protein attributes
| Sequence length | 476 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. |
| 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 – 476 | 476 | Cytochrome c oxidase subunit 1 | PRO_0000183396 | |||||||
Regions | |||||||||||
| Transmembrane | 19 – 39 | 21 | Helical; Potential | ||||||||
| Transmembrane | 61 – 81 | 21 | Helical; Potential | ||||||||
| Transmembrane | 105 – 125 | 21 | Helical; Potential | ||||||||
| Transmembrane | 151 – 171 | 21 | Helical; Potential | ||||||||
| Transmembrane | 194 – 214 | 21 | Helical; Potential | ||||||||
| Transmembrane | 240 – 260 | 21 | Helical; Potential | ||||||||
| Transmembrane | 278 – 298 | 21 | Helical; Potential | ||||||||
| Transmembrane | 310 – 330 | 21 | Helical; Potential | ||||||||
| Transmembrane | 345 – 365 | 21 | Helical; Potential | ||||||||
| Transmembrane | 379 – 399 | 21 | Helical; Potential | ||||||||
| Transmembrane | 415 – 435 | 21 | Helical; Potential | ||||||||
| Transmembrane | 455 – 475 | 21 | Helical; Potential | ||||||||
Sites | |||||||||||
| Metal binding | 66 | 1 | Iron (heme A axial ligand) Probable | ||||||||
| Metal binding | 246 | 1 | Copper B Probable | ||||||||
| Metal binding | 250 | 1 | Copper B Probable | ||||||||
| Metal binding | 295 | 1 | Copper B Probable | ||||||||
| Metal binding | 296 | 1 | Copper B Probable | ||||||||
| Metal binding | 382 | 1 | Iron (heme A3 axial ligand) Probable | ||||||||
| Metal binding | 384 | 1 | Iron (heme A axial ligand) Probable | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 246 ↔ 250 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity | |||||||||
Sequences
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References
| [1] | "Homologies between the contiguous and fragmented rRNAs of the two Plasmodium falciparum extrachromosomal DNAs are limited to core sequences." Feagin J.E., Werner E., Gardner M.J., Williamson D.H., Wilson R.J. Nucleic Acids Res. 20:879-887(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Molecular cloning and partial sequence of a 5.8 kilobase pair repetitive DNA from Plasmodium falciparum." Suplick K., Akella R., Saul A.J., Vaidya A. Mol. Biochem. Parasitol. 30:289-290(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MALAY CAMP. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M76611 Genomic DNA. Translation: AAC63390.2. Sequence problems. M99416 Genomic DNA. Translation: AAC06269.1. Sequence problems. |
3D structure databases | |
| ProteinModelPortal | Q02766. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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. [Graphical view] |
| PANTHER | PTHR10422. PTHR10422. 1 hit. |
| Pfam | PF00115. COX1. 1 hit. [Graphical view] |
| PRINTS | PR01165. CYCOXIDASEI. |
| SUPFAM | SSF81442. COX1. 1 hit. |
| PROSITE | PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX1_PLAFA | ||||||||
| Accession | Primary (citable) accession number: Q02766 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
