SMART: Pfam domain Complex1

The domain within your query sequence starts at position 1 and ends at position 173; the E-value for the Complex1_51K domain shown below is 3.6e-53.

MKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEGEPGTCKDREIMRHDPHKLV
EGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSDYDFDVFVVR
GAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSP

Complex1_51K

PFAM accession number:	PF01512
Interpro abstract (IPR011538):	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) ]. NADH:ubiquinone oxidoreductase (complex I) ( EC 1.6.5.3 ) 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 represents the FMN-binding domain.

PFAM accession number:

PF01512

Interpro abstract (IPR011538):

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) ].

NADH:ubiquinone oxidoreductase (complex I) ( EC 1.6.5.3 ) 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 represents the FMN-binding domain.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Complex1_51K