ID A0A0D1ZCA7_9EURO Unreviewed; 631 AA.
AC A0A0D1ZCA7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=PV08_11626 {ECO:0000313|EMBL:KIW10662.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW10662.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW10662.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW10662.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) 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; KN847500; KIW10662.1; -; Genomic_DNA.
DR RefSeq; XP_016230878.1; XM_016385934.1.
DR AlphaFoldDB; A0A0D1ZCA7; -.
DR STRING; 91928.A0A0D1ZCA7; -.
DR GeneID; 27338709; -.
DR VEuPathDB; FungiDB:PV08_11626; -.
DR HOGENOM; CLU_009667_4_1_1; -.
DR OrthoDB; 275372at2759; -.
DR Proteomes; UP000053328; 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 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 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:UP000053328};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT DOMAIN 289..382
FT /note="ETF-QO/FixC ubiquinone-binding"
FT /evidence="ECO:0000259|Pfam:PF21162"
FT DOMAIN 525..629
FT /note="ETF-QO/FixX C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05187"
FT REGION 612..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 70403 MW; E1192F24E4E68E6E CRC64;
MASKHISRPL LRLSNPALQC RSFSRPAVPL TRAIPRQRRT TLRTTRPLFV AGQRRSISAS
LQRKYADVDE AFDPATIDRE SDEVDVCIVG AGPAGLSAAI RLKQLANEAG NEEFRVVVLE
KAGEVGAHML SGNVLEPRAI NELIPDWLAE DNENRFTGAT PAGSDKMRFL TKSGAIPIPA
PPQMHNKGNY IISLSQFVKW LGERAEEIGV EIYPGFSASE ILYNHEGAVK GIATNDQGVG
RDGKAKANFE RGMEFHARVT LLAEGCHGSL TKRVSKKYDL RRDCQPQTYG LGLKEVWEIQ
PEKFKKGEIA HTMGYPLNRN TYGGGWMYHF GDNLVSLGLV VGLDYSNPWI SPYGEFQRMK
LHPFYKSVLE GGKCIAYGAR ALNEGGFQSI PKCAFPGGAL IGDTAGFLNV PKIKGTHTSM
KSGILAAEAT YEALNSNKED STIFLYNYED SLRSSWIWPE LKQVRNMRPS FHNPLGLYGG
IMYSGLEAYI FRGMTPWTLR HKKPDWANTR PADEMPKIEY PKPDGEITFD ILTSVSRTNT
NHEEDQPVHL QVKDWDAHAQ MDYPKYKGVE NRFCPAGVYE YVEDETKDLG VRFQINAQNC
IHCKTCDIKD PSQDINWQTP QGGEGPSYSI T
//
