CellStructureMech

fumarate reductase complex

GO:0045283 · Energy complex · Multiprotein complex · Proposed

A membrane-bound four-subunit respiratory quinol:fumarate reductase complex whose extrinsic catalytic module and membrane-anchor module couple fumarate reduction to quinol oxidation. [GO:0045283]

Synonyms: quinol-fumarate reductase

UniProt location names: UniProt Consortium, CC BY 4.0. Reference label and route sources.

Components

ComponentTypePart of / acts onGroundingGenesStoichiometryEssentialRole
Fumarate reductase, flavoprotein subunitProteinpart ofInterPro:IPR005884frdAESSENTIALFAD-binding flavoprotein subunit in the membrane-extrinsic catalytic domain of the fumarate reductase complex.
  • InterPro:IPR005884 InterPro IPR005884 is the source-neutral family for the fumarate reductase flavoprotein subunit.
  • PDB:1KF6 RCSB maps PDB:1KF6 polymer entity 1 to the E. coli FrdA flavoprotein subunit, UniProtKB:P00363.
fumarate reductase iron-sulfur subunitProteinpart ofReviewed label only (reviewed name; no accession asserted)frdBESSENTIALIron-sulfur subunit in the membrane-extrinsic catalytic domain that links the flavoprotein to the FrdC/FrdD membrane anchor.
  • GO:0045283 GO:0045283 defines subunits A and B as the fumarate reductase membrane-extrinsic catalytic domain.
  • PDB:1KF6 RCSB maps PDB:1KF6 polymer entity 2 to the E. coli FrdB iron-sulfur subunit, UniProtKB:P0AC47.
Fumarate reductase, subunit CProteinpart ofInterPro:IPR003510frdCESSENTIALFifteen-kilodalton hydrophobic membrane-anchor subunit that helps link the catalytic centers of fumarate reductase to the respiratory electron-transfer chain.
  • InterPro:IPR003510 InterPro IPR003510 is the source-neutral family for Fumarate reductase, subunit C.
  • PDB:1KF6 RCSB maps PDB:1KF6 polymer entity 3 to the E. coli FrdC hydrophobic subunit, UniProtKB:P0A8Q0.
Fumarate reductase, subunit DProteinpart ofInterPro:IPR003418frdDESSENTIALThirteen-kilodalton hydrophobic membrane-anchor subunit that helps anchor the fumarate reductase catalytic module to the cytoplasmic membrane.
  • InterPro:IPR003418 InterPro IPR003418 is the source-neutral family for Fumarate reductase, subunit D.
  • PDB:1KF6 RCSB maps PDB:1KF6 polymer entity 4 to the E. coli FrdD hydrophobic subunit, UniProtKB:P0A8Q3.

Canonical examples

Functions

Mechanism graphs

Fumarate reductase couples quinol oxidation to fumarate reduction (FUNCTION)

The fumarate reductase FrdAB catalytic domain and FrdCD membrane anchor form a respiratory complex that oxidizes quinol and reduces fumarate during anaerobic electron transport.

SubjectPredicateObjectEvidence
fumarate reductase complexenablesquinol:fumarate reductase activity
  • GO:0045283 GO:0045283 defines the four-subunit fumarate reductase complex by quinol oxidation coupled to fumarate reduction.
Fumarate reductase, flavoprotein subunitassembles withfumarate reductase iron-sulfur subunit
  • GO:0045283 GO:0045283 states that subunits A and B comprise the fumarate reductase membrane-extrinsic catalytic domain.
Fumarate reductase, subunit Ccontributes tofumarate reductase complex
  • InterPro:IPR003510 InterPro IPR003510 defines Fumarate reductase, subunit C as a 15 kDa hydrophobic subunit of the four-subunit complex.
Fumarate reductase, subunit Dcontributes tofumarate reductase complex
  • InterPro:IPR003418 InterPro IPR003418 defines fumarate reductase subunit D as the 13 kDa hydrophobic subunit.
quinoldonates electrons toquinol:fumarate reductase activity
  • GO:0045283 GO:0045283 records quinol oxidation as coupled to fumarate reduction by the complex.
fumarateaccepts electrons inquinol:fumarate reductase activity
  • GO:0045283 GO:0045283 records fumarate reduction to succinate as part of the complex's reaction.
quinol:fumarate reductase activityproducesquinone
  • GO:0045283 GO:0045283 records quinone production as the oxidized side of the quinol:fumarate reaction.
quinol:fumarate reductase activityproducessuccinate
  • GO:0045283 GO:0045283 records succinate production as the reduced side of the quinol:fumarate reaction.

Discussions

Evidence

Curation history

Source: data/structures/energy_complex/fumarate_reductase_complex.yaml