ID J3JTE9_DENPD Unreviewed; 601 AA.
AC J3JTE9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=D910_09219 {ECO:0000313|EMBL:ERL91896.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:AEE61469.1};
RN [1] {ECO:0000313|EMBL:AEE61469.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole emerged adults {ECO:0000313|EMBL:AEE61469.1};
RX PubMed=22516182; DOI=10.1016/j.ibmb.2012.03.010;
RA Keeling C.I., Henderson H., Li M., Yuen M., Clark E.L., Fraser J.D.,
RA Huber D.P., Liao N.Y., Roderick Docking T., Birol I., Chan S.K.,
RA Taylor G.A., Palmquist D., Jones S.J., Bohlmann J.;
RT "Transcriptome and full-length cDNA resources for the mountain pine beetle,
RT Dendroctonus ponderosae Hopkins, a major insect pest of pine forests.";
RL Insect Biochem. Mol. Biol. 42:525-536(2012).
RN [2] {ECO:0000313|EMBL:ERL91896.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
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; BT126505; AEE61469.1; -; mRNA.
DR EMBL; KB632306; ERL91896.1; -; Genomic_DNA.
DR AlphaFoldDB; J3JTE9; -.
DR STRING; 77166.J3JTE9; -.
DR OrthoDB; 275372at2759; -.
DR Proteomes; UP000030742; 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; 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; PF12831; FAD_oxidored; 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 2: Evidence at transcript level;
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:UP000030742};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT DOMAIN 561..590
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 601 AA; 66302 MW; 66928B70A2A520AF CRC64;
MSFNSGHSIK IAKQLKYFTR CYSDLFPKIT THYTIHPRDK DPRWKEVNME RFADETDILI
VGGGPAGMSA AIRAKQLAEK DGKEVRVCLV EKASEVGGHI LSGAVIQPTA LNELIPDWQE
KGAPLKTPVK EDKFAFLTET GRIPIPVLPG TPMYNHGNYV VRLGHVVQWL GEQAEALGVE
IYPGYAASEV LYHEDGSVKG IATNDVGIAK DGSPKDNFER GMELHAKCTI FAEGCHGHLS
KQIINRFDLR KNAEHQTYGI GLKELWEINP DKHSPGRVEH SIGWPLDKNT YGGSFLYHLN
EDTPLVAVGF VVGLDYSNPY LSPFREFQKF KHHPSVKHYF EDGTRVAYGA RALIEGGFQS
IPKLTFPGGC LVGCAAGLIN LPKIKGTHNA MKSGMLAAES VYEAINGEKQ KTEGFQPITY
EETFKNSWIY KELKAVRNIR PSFHNPLGLY GGLAYSGFSV VVGGREPWTL KHGDPDHKRL
KPAKECKPIE YPKPDGKISF DLLTSVALTG TNHEGDQPAH LTLKDDTVPV NHNLAVFDGP
EGRFCPAGVY EFVSLETGDG QRLQINAQNC IHCKTCDIKD PSQNINWVVP EGGGGPAYNG
M
//
