Reviewed,
UniProtKB/Swiss-Prot Q6NFM3 (COX1_CORDI)
Last modified
February 9, 2010.
Version 47.
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 oxidase subunit 1 EC=1.9.3.1 Alternative name(s): Cytochrome c oxidase polypeptide I Cytochrome aa3 subunit 1 | ||||
| Gene names |
| ||||
| Organism | Corynebacterium diphtheriae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1717 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 564 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. |
| Cofactor | Binds 1 copper B per subunit By similarity. Binds 2 heme groups per subunit By similarity. |
| Pathway | |
| Subunit structure | Associates with subunits II, III and IV to form cytochrome c oxidase By similarity. |
| Subcellular location | Cell membrane; Multi-pass membrane protein By similarity. |
| 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 – 564 | 564 | Cytochrome c oxidase subunit 1 | PRO_0000183438 | |||||||
Regions | |||||||||||
| Transmembrane | 43 – 63 | 21 | Potential | ||||||||
| Transmembrane | 83 – 103 | 21 | Potential | ||||||||
| Transmembrane | 122 – 142 | 21 | Potential | ||||||||
| Transmembrane | 171 – 191 | 21 | Potential | ||||||||
| Transmembrane | 214 – 234 | 21 | Potential | ||||||||
| Transmembrane | 259 – 279 | 21 | Potential | ||||||||
| Transmembrane | 292 – 312 | 21 | Potential | ||||||||
| Transmembrane | 316 – 336 | 21 | Potential | ||||||||
| Transmembrane | 360 – 380 | 21 | Potential | ||||||||
| Transmembrane | 399 – 419 | 21 | Potential | ||||||||
| Transmembrane | 434 – 454 | 21 | Potential | ||||||||
| Transmembrane | 477 – 497 | 21 | Potential | ||||||||
Sites | |||||||||||
| Metal binding | 87 | 1 | Iron (heme A axial ligand) Probable | ||||||||
| Metal binding | 265 | 1 | Copper B Probable | ||||||||
| Metal binding | 269 | 1 | Copper B Probable | ||||||||
| Metal binding | 314 | 1 | Copper B Probable | ||||||||
| Metal binding | 315 | 1 | Copper B Probable | ||||||||
| Metal binding | 398 | 1 | Iron (heme A3 axial ligand) Probable | ||||||||
| Metal binding | 400 | 1 | Iron (heme A axial ligand) Probable | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 265 ↔ 269 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity | |||||||||
Sequences
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References
| [1] | "The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129." Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S. Parkhill J.Nucleic Acids Res. 31:6516-6523(2003) [PubMed: 14602910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700971 / NCTC 13129 / Biotype gravis. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX248359 Genomic DNA. Translation: CAE50393.1. |
| RefSeq | NP_940201.1. |
3D structure databases | |
| SMR | Q6NFM3. Positions 36-531. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2649239. |
| KEGG | cdi:DIP1864. |
| NMPDR | fig|257309.1.peg.1792. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG603668. |
| OMA | NQISTVF. |
| PhylomeDB | Q6NFM3. |
Enzyme and pathway databases | |
| BioCyc | CDIP257309:DIP1864-MONOMER. |
| BRENDA | 1.9.3.1. 20483. |
Family and domain databases | |
| InterPro | IPR000883. Cyt_c_oxidase_su1. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view] |
| Gene3D | G3DSA:1.20.210.10. COX1. 1 hit. |
| PANTHER | PTHR10422. COX1. 1 hit. |
| Pfam | PF00115. COX1. 1 hit. [Graphical view] |
| PRINTS | PR01165. CYCOXIDASEI. |
| 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_CORDI | ||||||||
| Accession | Primary (citable) accession number: Q6NFM3 | ||||||||
| Entry history |
| ||||||||
| 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


