P00400 (COX1_DROYA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 101.
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 | Drosophila yakuba (Fruit fly) [Complete proteome] | ||||
| Taxonomic identifier | 7245 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › ![]() |
Protein attributes
| Sequence length | 511 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. |
| Caution | There is no mitochondrial-type translation initiation codon present in frame in the sequence. In Ref.3, the authors suggest the presence of a novel start codon coding for either Pro or Ser in Drosophila CoI transcripts. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 511 | 511 | Cytochrome c oxidase subunit 1 | PRO_0000183329 | |||||||
Regions | |||||||||||
| Transmembrane | 15 – 35 | 21 | Helical; Potential | ||||||||
| Transmembrane | 54 – 74 | 21 | Helical; Potential | ||||||||
| Transmembrane | 100 – 120 | 21 | Helical; Potential | ||||||||
| Transmembrane | 143 – 163 | 21 | Helical; Potential | ||||||||
| Transmembrane | 181 – 201 | 21 | Helical; Potential | ||||||||
| Transmembrane | 232 – 252 | 21 | Helical; Potential | ||||||||
| Transmembrane | 266 – 286 | 21 | Helical; Potential | ||||||||
| Transmembrane | 303 – 323 | 21 | Helical; Potential | ||||||||
| Transmembrane | 336 – 356 | 21 | Helical; Potential | ||||||||
| Transmembrane | 378 – 398 | 21 | Helical; Potential | ||||||||
| Transmembrane | 412 – 432 | 21 | Helical; Potential | ||||||||
| Transmembrane | 450 – 470 | 21 | Helical; Potential | ||||||||
Sites | |||||||||||
| Metal binding | 59 | 1 | Iron (heme A axial ligand) Probable | ||||||||
| Metal binding | 238 | 1 | Copper B Probable | ||||||||
| Metal binding | 242 | 1 | Copper B Probable | ||||||||
| Metal binding | 288 | 1 | Copper B Probable | ||||||||
| Metal binding | 289 | 1 | Copper B Probable | ||||||||
| Metal binding | 374 | 1 | Iron (heme A3 axial ligand) Probable | ||||||||
| Metal binding | 376 | 1 | Iron (heme A axial ligand) Probable | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 238 ↔ 242 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genes for cytochrome c oxidase subunit I, URF2, and three tRNAs in Drosophila mitochondrial DNA." Clary D.O., Wolstenholme D.R. Nucleic Acids Res. 11:6859-6872(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The mitochondrial DNA molecular of Drosophila yakuba: nucleotide sequence, gene organization, and genetic code." Clary D.O., Wolstenholme D.R. J. Mol. Evol. 22:252-271(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2317.6 Ivory Coast. |
| [3] | "Comparative genomics of Drosophila mtDNA: Novel features of conservation and change across functional domains and lineages." Montooth K.L., Abt D.N., Hofmann J.W., Rand D.M. J. Mol. Evol. 69:94-114(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X03240 Genomic DNA. Translation: CAC14066.1. |
| PIR | ODFF1Y. A93488. |
| RefSeq | NP_006903.1. NC_001322.1. |
3D structure databases | |
| ProteinModelPortal | P00400. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 807622. |
| KEGG | dya:COX1. |
Organism-specific databases | |
| CTD | 4512. |
| FlyBase | FBgn0013179. Dyak\mt:CoI. |
Phylogenomic databases | |
| KO | K02256. |
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_DROYA | ||||||||
| Accession | Primary (citable) accession number: P00400 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
