Reviewed,
UniProtKB/Swiss-Prot Q2LCQ6 (COX1_DICCI)
Last modified
February 9, 2010.
Version 31.
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+2 EC=1.9.3.1 Alternative name(s): Cytochrome c oxidase polypeptide I+II | ||
| Gene names |
| ||
| Encoded on | Mitochondrion | ||
| Organism | Dictyostelium citrinum (Slime mold) | ||
| Taxonomic identifier | 361072 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium |
Protein attributes
| Sequence length | 773 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. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | In the N-terminal section; belongs to the heme-copper respiratory oxidase family. In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 773 | 773 | Cytochrome c oxidase subunit 1+2 | PRO_0000312386 | |||||||
Regions | |||||||||||
| Transmembrane | 41 – 61 | 21 | Potential | ||||||||
| Transmembrane | 87 – 111 | 25 | Potential | ||||||||
| Transmembrane | 130 – 150 | 21 | Potential | ||||||||
| Transmembrane | 173 – 193 | 21 | Potential | ||||||||
| Transmembrane | 211 – 231 | 21 | Potential | ||||||||
| Transmembrane | 262 – 278 | 17 | Potential | ||||||||
| Transmembrane | 290 – 310 | 21 | Potential | ||||||||
| Transmembrane | 335 – 355 | 21 | Potential | ||||||||
| Transmembrane | 362 – 382 | 21 | Potential | ||||||||
| Transmembrane | 396 – 416 | 21 | Potential | ||||||||
| Transmembrane | 444 – 464 | 21 | Potential | ||||||||
| Transmembrane | 483 – 503 | 21 | Potential | ||||||||
| Transmembrane | 555 – 575 | 21 | Potential | ||||||||
| Transmembrane | 604 – 624 | 21 | Potential | ||||||||
| Region | 1 – 491 | 491 | COX1 | ||||||||
| Region | 492 – 773 | 282 | COX2 | ||||||||
Sites | |||||||||||
| Metal binding | 85 | 1 | Iron (heme A axial ligand) By similarity | ||||||||
| Metal binding | 264 | 1 | Copper B By similarity | ||||||||
| Metal binding | 268 | 1 | Copper B By similarity | ||||||||
| Metal binding | 314 | 1 | Copper B By similarity | ||||||||
| Metal binding | 315 | 1 | Copper B By similarity | ||||||||
| Metal binding | 400 | 1 | Iron (heme A3 axial ligand) By similarity | ||||||||
| Metal binding | 402 | 1 | Iron (heme A axial ligand) By similarity | ||||||||
| Metal binding | 709 | 1 | Copper A By similarity | ||||||||
| Metal binding | 744 | 1 | Copper A By similarity | ||||||||
| Metal binding | 748 | 1 | Copper A By similarity | ||||||||
| Metal binding | 752 | 1 | Copper A By similarity | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 264 ↔ 268 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity | |||||||||
Sequences
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References
| [1] | "Mitochondrial genome evolution in the social amoebae." Heidel A.J., Gloeckner G. Mol. Biol. Evol. 25:1440-1450(2008) [PubMed: 18413355] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DQ336395 Genomic DNA. Translation: ABC60387.1. |
| RefSeq | YP_492636.1. |
3D structure databases | |
| SMR | Q2LCQ6. Positions 530-769. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3912629. |
Family and domain databases | |
| InterPro | IPR001505. Copper_CuA. IPR008972. Cupredoxin. IPR000883. Cyt_c_oxidase_su1. IPR014222. Cyt_c_oxidase_su2. IPR015964. Cyt_c_oxidase_su2-like_TM_dom. IPR002429. Cyt_c_oxidase_su2_C. IPR011759. Cyt_c_oxidase_su2_TM_dom. [Graphical view] |
| Gene3D | G3DSA:1.20.210.10. COX1. 1 hit. G3DSA:1.10.287.90. COX2_TM. 1 hit. G3DSA:2.60.40.420. Cupredoxin. 1 hit. |
| PANTHER | PTHR10422. COX1. 1 hit. |
| Pfam | PF00115. COX1. 1 hit. PF00116. COX2. 1 hit. PF02790. COX2_TM. 1 hit. [Graphical view] |
| PRINTS | PR01165. CYCOXIDASEI. |
| TIGRFAMs | TIGR02866. CoxB. 1 hit. |
| PROSITE | PS50855. COX1. 1 hit. PS00078. COX2. 1 hit. PS50857. COX2_CUA. 1 hit. PS50999. COX2_TM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX1_DICCI | ||||||||
| Accession | Primary (citable) accession number: Q2LCQ6 | ||||||||
| Entry history |
| ||||||||
| 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


