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Database: UniProt
Entry: A0A066VV44_TILAU
LinkDB: A0A066VV44_TILAU
Original site: A0A066VV44_TILAU 
ID   A0A066VV44_TILAU        Unreviewed;       673 AA.
AC   A0A066VV44;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=K437DRAFT_249041 {ECO:0000313|EMBL:KDN42400.1};
OS   Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX   NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN42400.1, ECO:0000313|Proteomes:UP000027361};
RN   [1] {ECO:0000313|EMBL:KDN42400.1, ECO:0000313|Proteomes:UP000027361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBC 951 {ECO:0000313|EMBL:KDN42400.1,
RC   ECO:0000313|Proteomes:UP000027361};
RG   DOE Joint Genome Institute;
RA   Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA   Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT   "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT   951.";
RL   Submitted (MAY-2014) 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};
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:KDN42400.1}.
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DR   EMBL; JMSN01000070; KDN42400.1; -; Genomic_DNA.
DR   RefSeq; XP_013242035.1; XM_013386581.1.
DR   AlphaFoldDB; A0A066VV44; -.
DR   STRING; 1037660.A0A066VV44; -.
DR   GeneID; 25263315; -.
DR   HOGENOM; CLU_009667_4_0_1; -.
DR   InParanoid; A0A066VV44; -.
DR   OMA; INFQNCV; -.
DR   OrthoDB; 275372at2759; -.
DR   Proteomes; UP000027361; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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; PF13450; NAD_binding_8; 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:UP000027361};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT   DOMAIN          633..662
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   673 AA;  72831 MW;  7A10FA490BB10A6F CRC64;
     MLSPTARRSA ALVAAARTSV SSPSSSHASR TANALQSCTR PAAAAHSSLT YSSSSSSVRR
     TVASVRSALA TRRHFITSTA AKRDVPDDDV DALFDLAKIE RVSDEADVVI VGGGPAGLSA
     AIRIKQLAEE KGEDIRVVLL EKGGEVGNHI LSGAVIQTNA LDELLPNWKE LGAPLNQPAT
     EDHMRFLTKN GSFPLPHPPQ MSNKGNYIVS LSRVVAWLGE QAEAAGVEIY PGFAGSSIIW
     DEGTNGEKKG IKGIVTNEIG LNKARQPKDT FEPGMEFRAP ITLFAEGAHG SCTQQLIREL
     GLREAVNADP QTYALGIKEV WKVKEDKHQP GCVTHSLGWP MDMRTYGGSW MYHMEDGMVS
     VGLVVALDYE NPYMSPFKEF QRMKHHPFFK DVLEGGECLA YGARVLNEGG YQSIPKLHFP
     GGALIGCAAG FVNVPKIKGT HNAMKSGMTA AEATVDAILA RRAASGESES ESSTERPGID
     LVDYKTKLDN TYVMQELKEV RNLRPSFHNP LGLYGGILYS GLDSLILKGR TPWTFHHKQE
     DYQATKPASQ CRPIDYPKPD GQLSFDILTS VSRTGTNHTD DQPVHLVVKQ ADYKGHVERN
     VGTYDGLLGR VCPAAVYEYV DAEEAGGEDA LGKKLVINSQ NCIHCKTCSI KTPDQSITWT
     VPEGGGGPKY SLT
//
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