ID F7VE29_9PROT Unreviewed; 537 AA.
AC F7VE29;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 ORFNames=ATPR_1628 {ECO:0000313|EMBL:GAA08624.1};
OS Acetobacter tropicalis NBRC 101654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=749388 {ECO:0000313|EMBL:GAA08624.1, ECO:0000313|Proteomes:UP000004319};
RN [1] {ECO:0000313|EMBL:GAA08624.1, ECO:0000313|Proteomes:UP000004319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101654 {ECO:0000313|EMBL:GAA08624.1,
RC ECO:0000313|Proteomes:UP000004319};
RX PubMed=21554859; DOI=10.1016/j.bbrc.2011.04.126;
RA Matsutani M., Hirakawa H., Nishikura M., Soemphol W., Ali I.A.I.,
RA Yakushi T., Matsushita K.;
RT "Increased number of Arginine-based salt bridges contributes to the
RT thermotolerance of thermotolerant acetic acid bacteria, Acetobacter
RT tropicalis SKU1100.";
RL Biochem. Biophys. Res. Commun. 409:120-124(2011).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA08624.1}.
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DR EMBL; BABS01000042; GAA08624.1; -; Genomic_DNA.
DR AlphaFoldDB; F7VE29; -.
DR Proteomes; UP000004319; Unassembled WGS sequence.
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 InterPro; IPR023753; FAD/NAD-binding_dom.
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; PF07992; Pyr_redox_2; 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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT DOMAIN 3..47
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 202..295
FT /note="ETF-QO/FixC ubiquinone-binding"
FT /evidence="ECO:0000259|Pfam:PF21162"
FT DOMAIN 433..533
FT /note="ETF-QO/FixX C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05187"
SQ SEQUENCE 537 AA; 59012 MW; 7E2AC0A9CFA7F385 CRC64;
MEFDVVIVGG GPAGLAAAIR LRQLSPETSV CLIEKGSEIG AHIVSGAVIE PRALAELLPD
WKERGAPLNT AVTAEEMLYL TETGSVRVPF LDKLMPHMAN HGNYIVSLGE VCRWLATQAE
ELGVEIYPGF AGAEVLIENN RVAGVATGDM GITREGEHGS NYQPGMELRG RYTLFAEGCR
GSLTKQVMAH YDLRKGVDPQ TYGLGIKEVW EIPAEKHRPG LVQHSFGWPL DDQTYGGAWL
YHFGENLVSY GFVVGLDYPN TWLSPFEEMQ RLKLHPAFRK HLEGGRRVSY GARALSEGGL
QAVPRLTFPG GALIGDSAGF LNVPKIKGTH TAMKSGMLAA EAVVEALASN RPEPASFTQR
VKDSWLWEEL RTARNIRPAF ARFGMKKGAI YAGIDAMLLK GRAPWTLHFK HQDNEVLKPA
SLCEKPAYPK PDGQLTFDRL SSVFLSATNH EEDQPVHLRV KNLSLWKTVN WDVFRAPESR
YCPAGVYEVV DEATDPRLQI NAQNCVHCKT CDIKDPAQNI DWAVPEGGGG PNYPAGM
//
