Summary: Succinate dehydrogenase/Fumarate reductase transmembrane subunit
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Fumarate reductase Edit Wikipedia article
|Fumarate reductase respiratory complex|
Structure of Quinol-Fumarate Reductase Flavoprotein Subunit A.
|Fumarate reductase subunit C|
quinol-fumarate reductase with menaquinol molecules
|Fumarate reductase subunit D|
quinol-fumarate reductase with quinol inhibitor 2-[1-(4-chloro-phenyl)-ethyl]-4,6-dinitro-phenol
Succinate + acceptor <=> fumarate + reduced acceptor
In other words, fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase).
Fumarate reductase complex includes three subunits. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules. The D subunit may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.
- Lancaster CR, Sauer US, Gross R, et al. (December 2005). "Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase". Proc. Natl. Acad. Sci. U.S.A. 102 (52): 18860–5. doi:10.1073/pnas.0509711102. PMC 1323215. PMID 16380425.
- Iverson TM, Luna-Chavez C, Cecchini G, Rees DC (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex". Science 284 (5422): 1961–6. doi:10.1126/science.284.5422.1961. PMID 10373108.
- Michel H, Lancaster CR, Kroger A, Auer M (1999). "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution". Nature 402 (6760): 377–385. doi:10.1038/46483. PMID 10586875.
- Fumarate reductase / succinate dehydrogenase FAD-binding site in PROSITE
- Fumarate Reductase at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 188.8.131.52
Succinate dehydrogenase/Fumarate reductase transmembrane subunit Provide feedback
This family includes a transmembrane protein from both the Succinate dehydrogenase and Fumarate reductase complexes.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000701
This entry includes the transmembrane subunit from both succinate dehydrogenase and fumarate reductase complexes.
Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase) [PUBMED:10586875]. Three protein subunits contain the fumarate reductase complex. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules [PUBMED:10586875].
Succinate dehydrogenase (SDH) is a membrane-bound complex of two main components: a membrane-extrinsic component composed of an FAD-binding flavoprotein and an iron-sulphur protein, and a hydrophobic component composed of a cytochrome b and a membrane anchor protein. The cytochrome b component is a mono-haem transmembrane protein [PUBMED:1447196, PUBMED:8152421, PUBMED:7616569] belonging to a family that includes:
- Cytochrome b-556 from bacterial SDH (gene sdhC).
- Cytochrome b560 from the mammalian mitochondrial SDH complex, which is encoded in the mitochondrial genome of some algae and in the plant Marchantia polymorpha.
- Cytochrome b from yeast mitochondrial SDH complex (gene SDH3 or CYB3).
- Protein cyt-1 from Caenorhabditis elegans.
These cytochromes are proteins of about 130 residues that comprise three transmembrane regions. There are two conserved histidines which may be involved in binding the haem group.
|Molecular function||oxidoreductase activity, acting on the CH-CH group of donors (GO:0016627)|
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This superfamily constitutes two distinct families: in one family the common fold is contained in a single-chain subunit, in the other it is formed by two chains.
The clan contains the following 5 members:CybS DUF1691 Fumarate_red_C Fumarate_red_D Sdh_cyt
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|Seed source:||Prosite & Structural domain|
|Author:||Finn RD, Bateman A, Griffiths-Jones SR|
|Number in seed:||125|
|Number in full:||5134|
|Average length of the domain:||114.00 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||77.37 %|
|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:||17|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 Sdh_cyt domain has been found. There are 88 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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