ID A0A1M7J8L8_9GAMM Unreviewed; 538 AA.
AC A0A1M7J8L8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05428972_3787 {ECO:0000313|EMBL:SHM49345.1};
OS Rhodanobacter sp. OK091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1881037 {ECO:0000313|EMBL:SHM49345.1, ECO:0000313|Proteomes:UP000184078};
RN [1] {ECO:0000313|EMBL:SHM49345.1, ECO:0000313|Proteomes:UP000184078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK091 {ECO:0000313|EMBL:SHM49345.1,
RC ECO:0000313|Proteomes:UP000184078};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000256|ARBA:ARBA00002819, 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; FRCH01000006; SHM49345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7J8L8; -.
DR STRING; 1881037.SAMN05428972_3787; -.
DR OrthoDB; 9766632at2; -.
DR Proteomes; UP000184078; 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; IPR017896; 4Fe4S_Fe-S-bd.
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; PF01946; Thi4; 1.
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.
DR PROSITE; PS51379; 4FE4S_FER_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000184078};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT DOMAIN 498..527
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 538 AA; 58234 MW; 0D246A6D0551069A CRC64;
MSDRETMEYD VVVVGAGPAG LSFAIRLKQL KPEVSVCVIE KASTIGAQIL SGAVIEPQPL
DALLPGWRDN PPPICVPAGE DEFWLLSKTS GRKLPVPPGM HNHGNFIVSL GAMCAWLAPQ
AEALGVDVFP GFAAADTIYN EDGSVAGVRI GDMGVAKDGT HKPGYTEGID IKAKVTVLAE
GARGSLTKQL IKRFKLDADS DPQGYSIGIK ELWQLPPGRV TPGKIVHSFG WPADTHTYGG
SFLYHLDQDR VALGYVSGLD YSDPNYQPWE AFQQWKNHPT VKPLLDGGTI LSAGARAIVT
GGYQSLPKTE MPGALLIGDT AGLLNVPKVK GTHQAIKSGM LAAEHLVAHG LDSAGFDAKL
RGSDVMAELR KVRNIKPAFK KGLWFGMLNA AWETVTGGIS PWTLKNKADW SSLHKLGAQE
EPKRDYVQRT LAPRDRLAGV YFAATEHDED QPIHLHVADT RICIDQCTTE YGNPCTRFCP
ANVYEIVEDV HADGSKGRRL QINAANCVHC KTCDIKDPYE IITWLTPEGG SGPNYQNL
//
