ID   ETFD_PARDE              Reviewed;          31 AA.
AC   P55932;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   02-SEP-2026, entry version 60.
DE   RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase;
DE            Short=ETF-QO;
DE            Short=ETF-ubiquinone oxidoreductase;
DE            EC=1.5.5.1 {ECO:0000250|UniProtKB:Q16134};
DE   AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE            Short=ETF dehydrogenase;
DE   Flags: Fragment;
OS   Paracoccus denitrificans.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8306995; DOI=10.1111/j.1432-1033.1994.tb19939.x;
RA   Goodman S.I., Axtell K.M., Bindoff L.A., Beard S.E., Gill R.E.,
RA   Frerman F.E.;
RT   "Molecular cloning and expression of a cDNA encoding human electron
RT   transfer flavoprotein-ubiquinone oxidoreductase.";
RL   Eur. J. Biochem. 219:277-286(1994).
CC   -!- FUNCTION: Transfers electrons from the electron transfer flavoprotein
CC       (ETF) to ubiquinone. {ECO:0000250|UniProtKB:Q16134}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a
CC         ubiquinol + oxidized [electron-transfer flavoprotein] + H(+);
CC         Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307; EC=1.5.5.1;
CC         Evidence={ECO:0000250|UniProtKB:Q16134};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24053;
CC         Evidence={ECO:0000250|UniProtKB:Q16134};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q16134};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q16134};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q16134};
CC   -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
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DR   AlphaFoldDB; P55932; -.
DR   SMR; P55932; -.
DR   GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; FAD; Flavoprotein;
KW   Iron; Iron-sulfur; Lipid degradation; Lipid metabolism; Metal-binding;
KW   Oxidoreductase; Transport; Ubiquinone.
FT   CHAIN           1..>31
FT                   /note="Electron transfer flavoprotein-ubiquinone
FT                   oxidoreductase"
FT                   /id="PRO_0000200682"
FT   BINDING         19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P55931"
FT   NON_TER         31
SQ   SEQUENCE   31 AA;  2975 MW;  DAB2A13A3967D27D CRC64;
     SDIGGSMDYD VVIVGAGGAG LSAAILKQVN P
//