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Identification |
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Name | Cytochrome c oxidase subunit 2 |
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Synonyms | - Cytochrome c oxidase polypeptide II
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Gene Name | COX2 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in copper ion binding |
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Specific 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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1 |
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Cellular Location | Mitochondrion inner membrane; Multi-pass membrane protein |
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SMPDB Pathways | |
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KEGG Pathways | |
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SMPDB Reactions | Not Available |
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KEGG Reactions | Not Available |
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Metabolites | YMDB ID | Name | View |
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YMDB00862 | hydron | Show |
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GO Classification | Component |
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cell part | membrane | membrane part | intrinsic to membrane | integral to membrane | Function |
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electron carrier activity | catalytic activity | heme-copper terminal oxidase activity | cytochrome-c oxidase activity | copper ion binding | binding | ion binding | cation binding | metal ion binding | transition metal ion binding | iron ion binding | oxidoreductase activity | heme binding | Process |
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generation of precursor metabolites and energy | metabolic process | electron transport chain | respiratory electron transport chain | cellular metabolic process |
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Gene Properties |
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Chromosome Location | chromosome 17 |
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Locus | Q0250 |
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Gene Sequence | >756 bp
ATGTTAGATTTATTAAGATTACAATTAACAACATTCATTATGAATGATGTACCAACACCT
TATGCATGTTATTTTCAGGATTCAGCAACACCAAATCAAGAAGGTATTTTAGAATTACAT
GATAATATTATGTTTTATTTATTAGTTATTTTAGGTTTAGTATCTTGAATGTTATATACA
ATTGTTATAACATATTCAAAAAATCCTATTGCATATAAATATATTAAACATGGACAAACT
ATTGAAGTTATTTGAACAATTTTTCCAGCTGTAATTTTATTAATTATTGCTTTTCCTTCA
TTTATTTTATTATATTTATGTGATGAAGTTATTTCACCAGCTATAACTATTAAAGCTATT
GGATATCAATGATATTGAAAATATGAATATTCAGATTTTATTAATGATAGTGGTGAAACT
GTTGAATTTGAATCATATGTTATTCCTGATGAATTATTAGAAGAAGGTCAATTAAGATTA
TTAGATACTGATACTTCTATAGTTGTACCTGTAGATACACATATTAGATTCGTTGTAACA
GCTGCTGATGTTATTCATGATTTTGCTATTCCAAGTTTAGGTATTAAAGTTGATGCTACT
CCTGGTAGATTAAATCAAGTTTCTGCTTTAATTCAAAGAGAAGGTGTCTTCTATGGAGCA
TGTTCTGAGTTGTGTGGGACAGGTCATGCAAATATGCCAATTAAGATCGAAGCAGTATCA
TTACCTAAATTTTTGGAATGATTAAATGAACAATAA |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 251 |
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Protein Molecular Weight | 28566.90039 |
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Protein Theoretical pI | 4.2 |
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Signalling Regions | |
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Transmembrane Regions | |
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Protein Sequence | >Cytochrome c oxidase subunit 2
MLDLLRLQLTTFIMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYT
IVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEVISPAMTIKAI
GYQWYWKYEYSDFINDSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVT
AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGACSELCGTGHANMPIKIEAVS
LPKFLEWLNEQ |
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References |
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External Links | |
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General Reference | - Coruzzi, G., Tzagoloff, A. (1979). "Assembly of the mitochondrial membrane system. DNA sequence of subunit 2 of yeast cytochrome oxidase." J Biol Chem 254:9324-9330.225327
- Fox, T. D. (1979). "Five TGA "stop" codons occur within the translated sequence of the yeast mitochondrial gene for cytochrome c oxidase subunit II." Proc Natl Acad Sci U S A 76:6534-6538.230513
- Foury, F., Roganti, T., Lecrenier, N., Purnelle, B. (1998). "The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae." FEBS Lett 440:325-331.9872396
- Cameron, V. L., Fox, T. D., Poyton, R. O. (1989). "Isolation and characterization of a yeast strain carrying a mutation in the mitochondrial promoter for COX2." J Biol Chem 264:13391-13394.2547760
- Macino, G., Coruzzi, G., Nobrega, F. G., Li, M., Tzagoloff, A. (1979). "Use of the UGA terminator as a tryptophan codon in yeast mitochondria." Proc Natl Acad Sci U S A 76:3784-3785.226981
- Geier, B. M., Schagger, H., Ortwein, C., Link, T. A., Hagen, W. R., Brandt, U., Von Jagow, G. (1995). "Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method." Eur J Biochem 227:296-302.7851399
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