Reviewed,
UniProtKB/Swiss-Prot P24010 (COX1_BACSU)
Last modified
June 16, 2009.
Version 84.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
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 Caa-3605 subunit 1 Oxidase aa(3) subunit 1 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 622 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. |
| Catalytic activity | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O. |
| Cofactor | Binds 1 copper B ion per subunit. Binds 2 heme groups per subunit. |
| 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 – 622 | 622 | Cytochrome c oxidase subunit 1 | PRO_0000183436 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 27 | 27 | Extracellular Potential | ||||||||
| Transmembrane | 28 – 46 | 19 | Potential | ||||||||
| Topological domain | 47 – 68 | 22 | Cytoplasmic Potential | ||||||||
| Transmembrane | 69 – 88 | 20 | Potential | ||||||||
| Topological domain | 89 – 110 | 22 | Extracellular Potential | ||||||||
| Transmembrane | 111 – 128 | 18 | Potential | ||||||||
| Topological domain | 129 – 159 | 31 | Cytoplasmic Potential | ||||||||
| Transmembrane | 160 – 178 | 19 | Potential | ||||||||
| Topological domain | 179 – 196 | 18 | Extracellular Potential | ||||||||
| Transmembrane | 197 – 215 | 19 | Potential | ||||||||
| Topological domain | 216 – 241 | 26 | Cytoplasmic Potential | ||||||||
| Transmembrane | 242 – 261 | 20 | Potential | ||||||||
| Topological domain | 262 – 284 | 23 | Extracellular Potential | ||||||||
| Transmembrane | 285 – 304 | 20 | Potential | ||||||||
| Topological domain | 305 – 312 | 8 | Cytoplasmic Potential | ||||||||
| Transmembrane | 313 – 331 | 19 | Potential | ||||||||
| Topological domain | 332 – 346 | 15 | Extracellular Potential | ||||||||
| Transmembrane | 347 – 366 | 20 | Potential | ||||||||
| Topological domain | 367 – 374 | 8 | Cytoplasmic Potential | ||||||||
| Transmembrane | 375 – 394 | 20 | Potential | ||||||||
| Topological domain | 395 – 421 | 27 | Extracellular Potential | ||||||||
| Transmembrane | 422 – 441 | 20 | Potential | ||||||||
| Topological domain | 442 – 459 | 18 | Cytoplasmic Potential | ||||||||
| Transmembrane | 460 – 479 | 20 | Potential | ||||||||
| Topological domain | 480 – 552 | 73 | Extracellular Potential | ||||||||
| Transmembrane | 553 – 572 | 20 | Potential | ||||||||
| Topological domain | 573 – 580 | 8 | Cytoplasmic Potential | ||||||||
| Transmembrane | 581 – 604 | 24 | Potential | ||||||||
| Topological domain | 605 – 622 | 18 | Cytoplasmic Potential | ||||||||
Sites | |||||||||||
| Metal binding | 73 | 1 | Iron (heme A axial ligand) Probable | ||||||||
| Metal binding | 249 | 1 | Copper B Probable | ||||||||
| Metal binding | 253 | 1 | Copper B Probable | ||||||||
| Metal binding | 298 | 1 | Copper B Probable | ||||||||
| Metal binding | 299 | 1 | Copper B Probable | ||||||||
| Metal binding | 384 | 1 | Iron (heme A3 axial ligand) Probable | ||||||||
| Metal binding | 386 | 1 | Iron (heme A axial ligand) Probable | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 249 ↔ 253 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 120 | 1 | G → H in CAB11343. Ref.2 | ||||||||
| Sequence conflict | 155 – 156 | 2 | FV → SI in CAA38077. Ref.1 | ||||||||
| Sequence conflict | 288 | 1 | Missing in CAA38077. Ref.1 | ||||||||
| Sequence conflict | 474 | 1 | A → R in CAA38077. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved protein theme." Saraste M., Metso T., Nakari T., Jalli T., Lauraeus M., van der Oost J. Eur. J. Biochem. 195:517-525(1991) [PubMed: 1847686] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "Bacillus subtilis chromosomal region downstream nprE." Bertero M., Presecan E., Glaser P., Richou A., Danchin A. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [4] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 0:0-0(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 120. |
Cross-references
Sequence databases | |
|---|---|
| X54140 Genomic DNA. Translation: CAA38077.1. Z98682 Genomic DNA. Translation: CAB11343.1. AL009126 Genomic DNA. Translation: CAB13363.2. | |
| PIR | E69609. |
| RefSeq | NP_389373.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FFT based on UniProtKB P18401. |
| ModBase | Search... |
Protein family/group databases | |
| TCDB | 3.D.4.4.1. proton-translocating cytochrome oxidase (COX) superfamily. |
Genome annotation databases | |
| GeneID | 936898. |
| GenomeReviews | Gene locus BSU14900 in contig AL009126_GR. |
| KEGG | bsu:BSU14900. |
| NMPDR | fig|224308.1.peg.1492. |
Organism-specific databases | |
| SubtiList | BG10216. ctaD. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P24010. |
| OMA | P24010. IFAVATM. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU1492-MON. |
| BRENDA | 1.9.3.1. 150. |
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_BACSU | ||||||||
| Accession | Primary (citable) accession number: P24010 Secondary accession number(s): O34467 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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