Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodothermus marinus | - |
- |
- |
Rhodothermus marinus PRQ62b | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
lipoprotein | post-translational modification covalently binds a lipid to the cysteine residue included in the lipobox segment | Rhodothermus marinus |
proteolytic modification | sequence contains an N-terminal signal sequence of 26 amino acids | Rhodothermus marinus |
Subunits | Comment | Organism |
---|---|---|
? | x * 18000, SDS-PAGE of subunit ActE, truncated protein lacking 26 amino acid signal sequence | Rhodothermus marinus |
Synonyms | Comment | Organism |
---|---|---|
ActE | - |
Rhodothermus marinus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | covalently bound heme | Rhodothermus marinus |
General Information | Comment | Organism |
---|---|---|
physiological function | subunit ActE of alternative complex III functions as a direct electron donor to the cytochrome c aa3 oxygen reductase. The reduction potential of ActE is +165 mV, at pH 7.5 | Rhodothermus marinus |