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Overview for MACiE Entry M0281

Version history

General Information

EC Number: 1.5.5.1 (A member of the Oxidoreductases, Acting on the CH-NH group of donors, With a quinone or similar compound as acceptor)

Enzyme Name: electron-transferring-flavoprotein dehydrogenase

Biological Species: Sus scrofa (Pig)

Catalytic Chain UniprotKB Accession Codes:

  • P55931 - Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial

Representative PDB Code: 2gmh - STRUCTURE OF PORCINE ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE IN COMPLEXED WITH UBIQUINONE (Resolution = 2.50 Å).

Catalytic CATH Codes:

  • Unassigned Domain

Display structure information

Overall Reaction:

Image of ubiquinone

Image of reduced electron transfer flavoprotein

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Image of oxidised electron transfer flavoprotein

Image of ubiquinol

ubiquinone
C00399
CHEBI:16389
reduced electron transfer flavoprotein
C04570
oxidised electron transfer flavoprotein
C04253
CHEBI:30527
ubiquinol
C00390
CHEBI:17976

Overall Comment: Electron transfer flavoprotein-ubiquinone oxidoreductase is oxidised by the diffusible ubiquinone. The ubiquinol product relays electrons onto complex III. The enzyme links electrons from the oxidations of fatty acids to the mitochondrial respiratory chain.


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Stepwise Description of the Reaction

Step 1The reduced electron transfer flavoprotein delivers electron to the FAD cofactor via the iron sulfur cluster.
Step 2The oxidised electron transfer flavoprotein donates a proton to the FAD cofactor
Step 3The one electron oxidised electron transfer flavoprotein donates a second electron to the iron sulfur cluster, reducing its overall charge from +2 to +1.
Step 4The semiquinone FAD intermediate reduces the bound ubiquinone substrate.
Step 5The electron held by the iron sulfur cluster is now transferred to the FAD cofactor.
Step 6The oxidised electron transfer flavoprotein donates a proton to the FAD cofactor
Step 7FAD now donates a second reducing equivalent to the ubiquinone, forming the quinol product and regenerating the cofactor.

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Catalytic Residues Involved

Type Number Chain Location of Function
Arg 331 A Side Chain
Main Chain Carbonyl
Thr 367 A Side Chain
Ser 82 A Side Chain
Cys 553 A Side Chain
Cys 559 A Side Chain
Cys 556 A Side Chain
Main Chain Carbonyl
Cys 527 A Side Chain

Organic Cofactors for M0281

Type Identity Chain
FAD FAD 611 A Overview

Metal Cofactors for M0281

Type Het group Number Chain
iron SF4 610 A Overview

References

  1. J. Zhang et al. (2006), Proc. Natl Acad. Sci. USA, 103, 16212-16217. Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool.
    Medline: 17050691
  2. M. A. Swanson et al. (2008), Biochemistry, 47, 8894-8901. The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein.
    Medline: 18672901

Homologue information for M0281 (2gmh)

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

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electron-transferring-flavoprotein dehydrogenase activity (molecular function)
mitochondrial inner membrane (cellular component)
transport (biological process)
response to oxidative stress (biological process)
electron carrier activity (molecular function)
membrane (cellular component)
oxidoreductase activity (molecular function)
electron transport chain (biological process)
oxidoreductase activity, oxidizing metal ions with flavin as acceptor (molecular function)
mitochondrial part (cellular component)
metal ion binding (molecular function)
ubiquinone binding (molecular function)
flavin adenine dinucleotide binding (molecular function)
iron-sulfur cluster binding (molecular function)
4 iron, 4 sulfur cluster binding (molecular function)
oxidation-reduction process (biological process)
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