NADH-G_4Fe-4S_3NADH-ubiquinone oxidoreductase-G iron-sulfur binding region
|SMART accession number:||SM00929|
|Interpro abstract (IPR019574):|
NADH:ubiquinone oxidoreductase (complex I) (EC 126.96.36.199) is a respiratory-chain enzyme that catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane (NADH + ubiquinone = NAD+ + ubiquinol) [(PUBMED:1470679)]. Complex I is a major source of reactive oxygen species (ROS) that are predominantly formed by electron transfer from FMNH(2). Complex I is found in bacteria, cyanobacteria (as a NADH-plastoquinone oxidoreductase), archaea [(PUBMED:10940377)], mitochondria, and in the hydrogenosome, a mitochondria-derived organelle. In general, the bacterial complex consists of 14 different subunits, while the mitochondrial complex contains homologues to these subunits in addition to approximately 31 additional proteins [(PUBMED:18394423)].
This entry describes the G subunit (one of 14 subunits, A to N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This family does not contain related subunits from formate dehydrogenase complexes.
This entry represents the iron-sulphur binding domain of the G subunit.
|GO process:||oxidation-reduction process (GO:0055114)|
|GO function:||oxidoreductase activity (GO:0016491)|
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- Evolution (species in which this domain is found)
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- Structure (3D structures containing this domain)
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