ID Q11ZY8_POLSJ Unreviewed; 561 AA.
AC Q11ZY8;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase {ECO:0000256|RuleBase:RU366068};
DE Short=ETF-QO {ECO:0000256|RuleBase:RU366068};
DE EC=1.5.5.1 {ECO:0000256|RuleBase:RU366068};
GN OrderedLocusNames=Bpro_5295 {ECO:0000313|EMBL:ABE47154.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OG Plasmid pPol338 {ECO:0000313|Proteomes:UP000001983}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE47154.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000256|RuleBase:RU366068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a
CC ubiquinol + H(+) + oxidized [electron-transfer flavoprotein];
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:0000256|RuleBase:RU366068};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU366068};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU366068};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU366068};
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DR EMBL; CP000318; ABE47154.1; -; Genomic_DNA.
DR RefSeq; WP_011486133.1; NC_007950.1.
DR AlphaFoldDB; Q11ZY8; -.
DR KEGG; pol:Bpro_5295; -.
DR eggNOG; COG0644; Bacteria.
DR eggNOG; COG2440; Bacteria.
DR HOGENOM; CLU_009667_4_1_4; -.
DR OrthoDB; 9766632at2; -.
DR Proteomes; UP000001983; Plasmid pPol338.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.30.9.90; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR049398; ETF-QO/FixC_UQ-bd.
DR InterPro; IPR007859; ETF-QO/FixX_C.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10617; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10617:SF107; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF05187; ETF_QO; 1.
DR Pfam; PF21162; ETFQO_UQ-bd; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|RuleBase:RU366068};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366068};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366068};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU366068};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU366068};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366068};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366068}; Plasmid {ECO:0000313|EMBL:ABE47154.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT DOMAIN 222..314
FT /note="ETF-QO/FixC ubiquinone-binding"
FT /evidence="ECO:0000259|Pfam:PF21162"
FT DOMAIN 457..558
FT /note="ETF-QO/FixX C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05187"
SQ SEQUENCE 561 AA; 60566 MW; C07066BEB0A520F7 CRC64;
MMPSSLLEQY GPRESMDYDV VVVGGGPGGL ATAIRLKQLA AEKGQDVSVV VLEKGSAPGA
HILSGAVMDP IALNELFPNW KAMGAPLNQP VSGDDVLFLT ETGAKRTPDF LVPDCFHNEG
NYVISLGALT QWLGAQAETL GVEIFPGFTA AEVLYNDNGS VKGVATGNLG IGKDGQPHEG
FQLGMELHAK YTIFSEGARG HLGKQLIARY KLDAGRDPQS HALGIKELWE IDPARAQPGR
VLHTAGWPMD SQTYGGGFLY HLEGNLVTLG FVTGLDYKNP WLSPFEEMQR WKTHPAIRAH
IEGGKRISYG ARAITAGGLL SLPKTVFPGG ALIGCDAGYL NAARIKGSHA AIKSGMLAAE
AAFDALAAGR SGDELSAYPT AFENSWLHTE LDQSRNFKQW FKKGSLVGAL MTGIEQWLLP
RLGIKRPPWT IHRTQADHAC LRPAAEMPQI SYPKPDGKLT FDRLSSVFIS NTNHEENQPA
HLTLKDASVP VRINLANYAG PESRYCPAGV YEFVKNDDDS DRLQINAQNC VHCKTCDIKD
PTQNIVWVTP EGGGGPNYAG M
//
