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PROSITE documentation PDOC00570 [for PROSITE entry PS00667]

Respiratory-chain NADH dehydrogenase subunit 1 signatures





Description

Respiratory-chain NADH dehydrogenase (EC 1.6.5.3) [1,2] (also known as complex I or NADH-ubiquinone oxidoreductase) is an oligomeric enzymatic complex located in the inner mitochondrial membrane which also seems to exist in the chloroplast and in cyanobacteria (as a NADH-plastoquinone oxidoreductase). Among the 25 to 30 polypeptide subunits of this bioenergetic enzyme complex there are fifteen which are located in the membrane part, seven of which are encoded by the mitochondrial and chloroplast genomes of most species. The most conserved of these organelle-encoded subunits is known as subunit 1 (gene ND1 in mitochondrion, and NDH1 in chloroplast) and seems to contain the ubiquinone binding site.

The ND1 subunit is highly similar to subunit 4 of Escherichia coli formate hydrogenlyase (gene hycD), subunit C of hydrogenase-4 (gene hyfC). Paracoccus denitrificans NQO8 and Escherichia coli nuoH NADH-ubiquinone oxidoreductase subunits also belong to this family [3].

We have developed two signature patterns based on conserved regions of this subunit.

Last update:

April 2006 / Patterns revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

COMPLEX1_ND1_1, PS00667; Respiratory-chain NADH dehydrogenase subunit 1 signature 1  (PATTERN)

COMPLEX1_ND1_2, PS00668; Respiratory-chain NADH dehydrogenase subunit 1 signature 2  (PATTERN)


References

1AuthorsRagan C.I.
SourceCurr. Top. Bioenerg. 15:1-36(1987).

2AuthorsWeiss H. Friedrich T. Hofhaus G. Preis D.
TitleThe respiratory-chain NADH dehydrogenase (complex I) of mitochondria.
SourceEur. J. Biochem. 197:563-576(1991).
PubMed ID2029890

3AuthorsWeidner U. Geier S. Ptock A. Friedrich T. Leif H. Weiss H.
TitleThe gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I.
SourceJ. Mol. Biol. 233:109-122(1993).
PubMed ID7690854



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