Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR002023 is a NADH-quinone oxidoreductase subunit E-like.
<p>Respiratory-chain NADH dehydrogenase ([ec:7.1.1.2]) [[cite:PUB00001392]] (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 is one with a molecular weight of 24 Kd (in mammals), which is a component of the iron-sulfur (IP) fragment of the enzyme. It seems to bind a 2Fe-2S iron-sulfur cluster. The 24 Kd subunit is nuclear encoded, as a precursor form with a transit peptide in mammals, and in Neurospora crassa. The 24 Kd subunit is highly similar to [[cite:PUB00000637], [cite:PUB00003309]]: Subunit E of Escherichia coli NADH-ubiquinone oxidoreductase (gene nuoE) and Subunit NQO2 of Paracoccus denitrificans NADH-ubiquinone oxidoreductase.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. | ||
| Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: NADH dehydrogenase [ubiquinone] gi|449513453|ref|XP_004164329.1| | 11 | ||
| – | NADH-quinone oxidoreductase, subunit E; TAIR: AT4G02580.1 NADH-ubiquinone oxidoreductase 24 kDa subunit; Swiss-Prot: sp|O22769|NDUV2_ARATH NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial; TrEMBL-Plants: tr|I3SGC8|I3SGC8_LOTJA Uncharacterized protein; Found in the gene: LotjaGi3g1v0007400 | 15 | ||
| – | NADH-quinone oxidoreductase, subunit E; TAIR: AT4G02580.1 NADH-ubiquinone oxidoreductase 24 kDa subunit; Swiss-Prot: sp|O22769|NDUV2_ARATH NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial; TrEMBL-Plants: tr|I3SGC8|I3SGC8_LOTJA Uncharacterized protein; Found in the gene: LotjaGi3g1v0007400 | 12 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 33.33 |