The domain within your query sequence starts at position 355 and ends at position 400; the E-value for the NADH_4Fe-4S domain shown below is 1.05e-22.



NADH-ubiquinone oxidoreductase-F iron-sulfur binding region
SMART accession number:SM00928
Description: -
Interpro abstract (IPR019575):

Among the many polypeptide subunits that make up complex I, there is one with a molecular weight of 51kDa (in mammals), which is the second largest subunit of complex I [ (PUBMED:2029890) ]. The 51kDa 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.

NADH:ubiquinone oxidoreductase (complex I) ( EC ) 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) ].

GO function:4 iron, 4 sulfur cluster binding (GO:0051539)
Family alignment:
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There are 22767 NADH_4Fe-4S domains in 22761 proteins in SMART's nrdb database.

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