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80  structures 3465  species 1  interaction 7525  sequences 28  architectures

Family: Oxidored_q6 (PF01058)

Summary: NADH ubiquinone oxidoreductase, 20 Kd subunit

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This is the Wikipedia entry entitled "NADH dehydrogenase". More...

NADH dehydrogenase Edit Wikipedia article

NADH dehydrogenase
Identifiers
EC number 1.6.99.3
CAS number 9079-67-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

NADH dehydrogenase (EC 1.6.99.3, 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.[1][2][3][4] This enzyme catalyses the following chemical reaction

NADH + H+ + acceptor \rightleftharpoons NAD+ + reduced acceptor

NADH dehydrogenase is a flavoprotein that contains iron-sulfur centres.

[edit] References

  1. ^ 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. PMID 4402556.
  2. ^ 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.
  3. ^ 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. PMID 4144655.
  4. ^ Kaniuga, Z. (1963). "The transformation of mitochondrial NADH dehydrogenase into NADH:Cytochrome c oxidoreductase". Biochim. Biophys. Acta 73: 550–564. PMID 14074130.

[edit] See also

[edit] External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

NADH ubiquinone oxidoreductase, 20 Kd subunit Provide feedback

No Pfam abstract.

Literature references

  1. Walker JE; , Q Rev Biophys 1992;25:253-324.: The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. PUBMED:1470679 EPMC:1470679

  2. Peterson GC, Souza AE, Parsons M; , Mol Biochem Parasitol 1993;58:63-70.: Characterization of a Trypanosoma brucei nuclear gene encoding a protein homologous to a subunit of bovine NADH:ubiquinone oxidoreductase (complex I). PUBMED:8459836 EPMC:8459836

  3. Arizmendi JM, Runswick MJ, Skehel JM, Walker JE; , FEBS Lett 1992;301:237-242.: NADH: ubiquinone oxidoreductase from bovine heart mitochondria. A fourth nuclear encoded subunit with a homologue encoded in chloroplast genomes. PUBMED:1577158 EPMC:1577158


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006137

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].

Among the many polypeptide subunits that make up complex I, there is one with a molecular weight of 20 kDa (in mammals) [PUBMED:1577158], which is a component of the iron-sulphur (IP) fragment of the enzyme. It seems to bind a 4Fe-4S iron-sulphur cluster. The 20 kDa subunit has been found to be nuclear encoded, as a precursor form with a transit peptide in mammals, and in Neurospora crassa. It is and chloroplast encoded in various higher plants (gene ndhK or psbG).

Gene Ontology

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Domain organisation

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Alignments

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  Seed
(169)
Full
(7525)
Representative proteomes NCBI
(4724)
Meta
(2053)
RP15
(667)
RP35
(1322)
RP55
(1707)
RP75
(2007)
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  Seed
(169)
Full
(7525)
Representative proteomes NCBI
(4724)
Meta
(2053)
RP15
(667)
RP35
(1322)
RP55
(1707)
RP75
(2007)
Alignment:
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  Seed
(169)
Full
(7525)
Representative proteomes NCBI
(4724)
Meta
(2053)
RP15
(667)
RP35
(1322)
RP55
(1707)
RP75
(2007)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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Pfam alignments:

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Curation and family details

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Seed source: Pfam-B_1345 (release 3.0)
Previous IDs: oxidored_q6;
Type: Family
Author: Finn RD, Bateman A
Number in seed: 169
Number in full: 7525
Average length of the domain: 123.50 aa
Average identity of full alignment: 33 %
Average coverage of the sequence by the domain: 48.57 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.1 21.1
Trusted cut-off 21.2 21.1
Noise cut-off 21.0 21.0
Model length: 131
Family (HMM) version: 17
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Species distribution

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Interactions

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NiFeSe_Hases

Structures

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_q6 domain has been found. There are 80 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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