Summary: Electron transfer flavoprotein-ubiquinone oxidoreductase
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Electron transfer flavoprotein-ubiquinone oxidoreductase Provide feedback
Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The two redox centres in the protein, FAD and a [4Fe4S] cluster, are present in a 64-kDa monomer .
Goodman SI, Axtell KM, Bindoff LA, Beard SE, Gill RE, Frerman FE; , Eur J Biochem 1994;219:277-286.: Molecular cloning and expression of a cDNA encoding human electron transfer flavoprotein-ubiquinone oxidoreductase. PUBMED:8306995 EPMC:8306995
Williams PA, Shaw LE; , J Bacteriol 1997;179:5935-5942.: mucK, a gene in Acinetobacter calcoaceticus ADP1 (BD413), encodes the ability to grow on exogenous cis,cis-muconate as the sole carbon source. PUBMED:9294455 EPMC:9294455
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007859Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) in the inner mitochondrial membrane accepts electrons from electron-transfer flavoprotein which is located in the mitochondrial matrix and reduces ubiquinone in the mitochondrial membrane. The two redox centres in the protein, FAD and a [4Fe4S] cluster, are present in a 64 kDa monomer [PUBMED:8306995].
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|Molecular function||electron-transferring-flavoprotein dehydrogenase activity (GO:0004174)|
|Biological process||oxidation-reduction process (GO:0055114)|
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Curation and family details
|Seed source:||Pfam-B_2305 (release 7.7)|
|Author:||Wood V, Bateman A|
|Number in seed:||73|
|Number in full:||1342|
|Average length of the domain:||109.60 aa|
|Average identity of full alignment:||47 %|
|Average coverage of the sequence by the domain:||19.70 %|
|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:||8|
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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 ETF_QO domain has been found. There are 4 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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