Summary: Fumarate reductase subunit C
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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 four 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 . 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.
- Iverson, T. M.; Luna-Chavez, C; Cecchini, G; Rees, D. C. (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex". Science. 284 (5422): 1961–6. doi:10.1126/science.284.5422.1961. PMID 10373108.
- Fumarate reductase / succinate dehydrogenase FAD-binding site in PROSITE
- Fumarate Reductase at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 22.214.171.124
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Fumarate reductase subunit C Provide feedback
Fumarate reductase is a membrane-bound flavoenzyme consisting of four subunits, A-B. A and B comprise the membrane-extrinsic catalytic domain and C and D link the catalytic centres to the electron-transport chain. This family consists of the 15kD hydrophobic subunit C.
Cole ST; , Eur J Biochem 1987;167:481-488.: Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris. Extensive sequence divergence of the membrane anchors and absence of an frd-linked ampC cephalosporinase gene. PUBMED:3308458 EPMC:3308458
Internal database links
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003510Fumarate reductase is a membrane-bound flavoenzyme consisting of four subunits, A-D. A and B comprise the membrane-extrinsic catalytic domain and C and D link the catalytic centres to the electron-transport chain. This family consists of the 15kDa hydrophobic subunit C. Members of this subfamily are classified as Type D as they contain two transmembrane subunits (C and D) and no heme groups. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centres, and the transmembrane subunit containing the electron donor (quinol). The quinone binding site resides in the transmembrane subunits.
Quinol:fumarate reductase (QFR) couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, the opposite reaction to that catalyzed by the related protein, succinate:quinine oxidoreductase (SQR). QFRs oxidize low potential quinols such as menaquinol and are involved in anaerobic respiration with fumarate as the terminal electron acceptor. SQR and QFR share a common subunit arrangement, composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits [PUBMED:10373108, PUBMED:11850430, PUBMED:3308458, PUBMED:15654871, PUBMED:15884941, PUBMED:11803023, PUBMED:10486141, PUBMED:11803024, PUBMED:9210286, PUBMED:15078221, PUBMED:11004459].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
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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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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Seed source:||Pfam-B_11568 (release 5.2)|
|Author:||Mian N, Bateman A|
|Number in seed:||41|
|Number in full:||203|
|Average length of the domain:||123.80 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||95.63 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||16|
|Download:||download the raw HMM for this family|
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There are 5 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 Fumarate_red_C domain has been found. There are 18 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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