NADH_4Fe-4SNADH-ubiquinone oxidoreductase-F iron-sulfur binding region
|SMART accession number:||SM00928|
|Interpro abstract (IPR019575):|
NADH:ubiquinone oxidoreductase (complex I) (EC 220.127.116.11) 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)].
Among the many polypeptide subunits that make up complex I, there is one with a molecular weight of 51 kDa (in mammals), which is the second largest subunit of complex I [(PUBMED:2029890)]. The 51 kDa subunit, as the corresponding bacterial subunit (Nqo1 in Thermus and NuoF in E. coli) [(PUBMED:12600193)], contains the NADH-binding site, the primary electron acceptor FMN-binding site, and a 4Fe-4S cluster [(PUBMED:16469879)].
This entry represents the iron-sulphur binding domain.
|GO function:||4 iron, 4 sulfur cluster binding (GO:0051539)|
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- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Structure (3D structures containing this domain)
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