Summary: NADH-Ubiquinone/plastoquinone (complex I), various chains
This is the Wikipedia entry entitled "NADH dehydrogenase". More...
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NADH dehydrogenase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
NADH dehydrogenase (EC 18.104.22.168, cytochrome c reductase, type 1 dehydrogenase, beta-NADH dehydrogenase dinucleotide, diaphorase, dihydrocodehydrogenase I dehydrogenase, dihydronicotinamide adenine dinucleotide dehydrogenase, diphosphopyridine diaphorase, DPNH diaphorase, NADH diaphorase, NADH hydrogenase, NADH oxidoreductase, NADH-menadione oxidoreductase, reduced diphosphopyridine nucleotide diaphorase) is an enzyme with systematic name NADH:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction
- NADH + H+ + acceptor NAD+ + reduced acceptor
NADH dehydrogenase is a flavoprotein that contains iron-sulfur centres.
- Adachi, K. and Okuyama, T. (1972). "Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes". Biochim. Biophys. Acta 268: 629–637. doi:10.1016/0005-2744(72)90266-5. PMID 4402556.
- Hatefi, Y., Ragan, C.I. and Galante, Y.M. (1985). "The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system". In Martonosi, A. The Enzymes of Biological Membranes 4 (2nd ed.). New York: Plenum Press. pp. 1–70.
- Hochstein, L.I. and Dalton, B.P. (1973). "Studies of a halophilic NADH dehydrogenase. I. Purification and properties of the enzyme". Biochim. Biophys. Acta 302: 216–228. doi:10.1016/0005-2744(73)90150-2. PMID 4144655.
- Kaniuga, Z. (1963). "The transformation of mitochondrial NADH dehydrogenase into NADH:Cytochrome c oxidoreductase". Biochim. Biophys. Acta 73: 550–564. doi:10.1016/0926-6569(63)90175-5. PMID 14074130.
NADH-Ubiquinone/plastoquinone (complex I), various chains Provide feedback
This family is part of complex I which catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane.
External database links
|Transporter classification:||3.D.1 3.D.9|
This tab holds annotation information from the InterPro database.
InterPro entry IPR001750
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], mitochondira, 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]. Mitochondrial complex I, which is located in the inner mitochondrial membrane, is the largest multimeric respiratory enzyme in the mitochondria, consisting of more than 40 subunits, one FMN co-factor and eight FeS clusters [PUBMED:18563446]. The assembly of mitochondrial complex I is an intricate process that requires the cooperation of the nuclear and mitochondrial genomes [PUBMED:18563446, PUBMED:17854760]. Mitochondrial complex I can cycle between active and deactive forms that can be distinguished by the reactivity towards divalent cations and thiol-reactive agents. All redox prosthetic groups reside in the peripheral arm of the L-shaped structure. The NADH oxidation domain harbouring the FMN cofactor is connected via a chain of iron-sulphur clusters to the ubiquinone reduction site that is located in a large pocket formed by the PSST and 49kDa subunits of complex I [PUBMED:18982432].
This domain is found in the NADH:ubiquinone oxidoreductase (complex I) and NADH-plastoquinone oxidoreductase [PUBMED:1470679].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||NADH dehydrogenase (ubiquinone) activity (GO:0008137)|
|Biological process||ATP synthesis coupled electron transport (GO:0042773)|
|oxidation-reduction process (GO:0055114)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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This superfamily contains proteins from the families Oxidored_q1 and NADHdeh_related. The Oxidored_q1 family is part of complex I which catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane. Many members of the NADHdeh_related family are archaeal and bacterial, indicating the evolutionary origins of ComplexI.
The clan contains the following 2 members:NADHdeh_related Oxidored_q1
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Curation and family details
|Seed source:||Pfam-B_4 (release 1.0)|
|Number in seed:||33|
|Number in full:||91875|
|Average length of the domain:||225.60 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||56.30 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Oxidored_q1 domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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