Reviewed,
UniProtKB/Swiss-Prot Q8FMT1 (COX1_COREF)
Last modified
June 16, 2009.
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 efficiens [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 152794 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 580 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 – 580 | 580 | Cytochrome c oxidase subunit 1 | PRO_0000183439 | |||||||
Regions | |||||||||||
| Transmembrane | 43 – 63 | 21 | Potential | ||||||||
| Transmembrane | 90 – 110 | 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] | "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens." Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T. Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395. |
Cross-references
Sequence databases | |
|---|---|
| BA000035 Genomic DNA. Translation: BAC19228.1. | |
| RefSeq | NP_739028.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FFT based on UniProtKB P18401. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1032090. |
| GenomeReviews | Gene locus CE2418 in contig BA000035_GR. |
| KEGG | cef:CE2418. |
| NMPDR | fig|196164.1.peg.2418. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8FMT1. |
| OMA | Q8FMT1. TIIKLRR. |
Enzyme and pathway databases | |
| BioCyc | CEFF196164:CE2418-MON. |
| BRENDA | 1.9.3.1. 277326. |
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_COREF | ||||||||
| Accession | Primary (citable) accession number: Q8FMT1 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


