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Database: UniProt
Entry: A0A1E3QRN0_9ASCO
LinkDB: A0A1E3QRN0_9ASCO
Original site: A0A1E3QRN0_9ASCO 
ID   A0A1E3QRN0_9ASCO        Unreviewed;       636 AA.
AC   A0A1E3QRN0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-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=BABINDRAFT_161303 {ECO:0000313|EMBL:ODQ80353.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ80353.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV454430; ODQ80353.1; -; Genomic_DNA.
DR   RefSeq; XP_018985681.1; XM_019128735.1.
DR   AlphaFoldDB; A0A1E3QRN0; -.
DR   STRING; 984486.A0A1E3QRN0; -.
DR   GeneID; 30146588; -.
DR   OrthoDB; 275372at2759; -.
DR   Proteomes; UP000094336; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
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:0071949; F:FAD binding; IEA:InterPro.
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; IPR002938; FAD-bd.
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; PF01494; FAD_binding_3; 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.
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:UP000094336};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT   DOMAIN          62..260
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          271..364
FT                   /note="ETF-QO/FixC ubiquinone-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21162"
FT   DOMAIN          512..633
FT                   /note="ETF-QO/FixX C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05187"
SQ   SEQUENCE   636 AA;  69703 MW;  8A5C03854004FAB4 CRC64;
     MRLGPCVRAL RMRAAPVRAF GTPRARALTR AFSTSPAARE TPFSQLPEEA REILSEERAA
     DEVDVVIVGG GPAGLATAIK LKQLDAEHGS GELRVVVLEK ASDMGLHTVS GAVLEPRALC
     ELFPDSEHYA EGHEIPLPQD LATLVTTDSM KFLTATGSIP LPHPPQMVNK GKNYIVSLNQ
     VVKYLAEQAE ELGVEVYPGI AVDELLVEED AVRGVATRDM GIAKDLSPKD SYERGMEFHA
     KMTVLAEGCH GSLTKKAISK FALRGKNNQT YGLGIKEVWE VAPEKFNKGF VGHTMGYPLS
     TDVYGGGFQY HFGDGLVAVG IVVGLDYANP WISPYQEFQK MKHHPFYKDT LTGGKCISYG
     ARALNEGGWQ SVPRLHFPGG VLVGCSAGFM NVPKIKGTHT AMKSGMLAAE TIFEALQEAE
     ESEEGILSPI NLEAYQKAYE GSWIHEELYG VRNVRPSFNS PLTLFGGMAY SGLTTMITKG
     KESWTFDHHK SDASCTKPAD QFTKIDYPKP DGVISFDILT SVSRTGTYHD DDEPCHLRLT
     VPGKEAKETV NDEETLRKHA EKSYPRFKGV EQRFCPAGVY EYVESKDVKD EKAGGVKFQI
     NSQNCIHCKT CDIKVPDQDI DWTVPEGGDG PKYVMT
//
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