ETFQO_ARATH
ID ETFQO_ARATH Reviewed; 633 AA.
AC O22854;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
DE Short=ETF-QO;
DE Short=ETF-ubiquinone oxidoreductase;
DE EC=1.5.5.1;
DE Flags: Precursor;
GN Name=ETFQO; OrderedLocusNames=At2g43400; ORFNames=T1O24;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16055629; DOI=10.1105/tpc.105.035162;
RA Ishizaki K., Larson T.R., Schauer N., Fernie A.R., Graham I.A.,
RA Leaver C.J.;
RT "The critical role of Arabidopsis electron-transfer flavoprotein:ubiquinone
RT oxidoreductase during dark-induced starvation.";
RL Plant Cell 17:2587-2600(2005).
RN [5]
RP FUNCTION.
RX PubMed=20501910; DOI=10.1105/tpc.110.075630;
RA Araujo W.L., Ishizaki K., Nunes-Nesi A., Larson T.R., Tohge T.,
RA Krahnert I., Witt S., Obata T., Schauer N., Graham I.A., Leaver C.J.,
RA Fernie A.R.;
RT "Identification of the 2-hydroxyglutarate and isovaleryl-CoA dehydrogenases
RT as alternative electron donors linking lysine catabolism to the electron
RT transport chain of Arabidopsis mitochondria.";
RL Plant Cell 22:1549-1563(2010).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=29348240; DOI=10.1105/tpc.17.00414;
RA Pedrotti L., Weiste C., Naegele T., Wolf E., Lorenzin F., Dietrich K.,
RA Mair A., Weckwerth W., Teige M., Baena-Gonzalez E., Droege-Laser W.;
RT "Snf1-RELATED KINASE1-controlled C/S1-bZIP signaling activates alternative
RT mitochondrial metabolic pathways to ensure plant survival in extended
RT darkness.";
RL Plant Cell 30:495-509(2018).
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone. May act
CC downstream of IVD and D2HGDH in the degradation of phytol or
CC chlorophyll during dark-induced senescence and sugar starvation.
CC {ECO:0000269|PubMed:16055629, ECO:0000269|PubMed:20501910}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Up-regulated by KIN10, by S1-bZIP specific dimers,
CC and also by C/S1 bZIP heterodimers. {ECO:0000269|PubMed:29348240}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:16055629}.
CC -!- INDUCTION: By dark-induced senescence. {ECO:0000269|PubMed:16055629}.
CC -!- DISRUPTION PHENOTYPE: Accelerated senescence and short siliques with
CC reduced seed number. {ECO:0000269|PubMed:16055629}.
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX819708; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AC002335; AAB64328.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10261.1; -; Genomic_DNA.
DR EMBL; BX819708; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F84865; F84865.
DR RefSeq; NP_181868.1; NM_129901.4.
DR AlphaFoldDB; O22854; -.
DR SMR; O22854; -.
DR STRING; 3702.AT2G43400.1; -.
DR PaxDb; O22854; -.
DR PRIDE; O22854; -.
DR ProteomicsDB; 222326; -.
DR EnsemblPlants; AT2G43400.1; AT2G43400.1; AT2G43400.
DR GeneID; 818941; -.
DR Gramene; AT2G43400.1; AT2G43400.1; AT2G43400.
DR KEGG; ath:AT2G43400; -.
DR Araport; AT2G43400; -.
DR TAIR; locus:2058183; AT2G43400.
DR eggNOG; KOG2415; Eukaryota.
DR HOGENOM; CLU_009667_4_1_1; -.
DR InParanoid; O22854; -.
DR OrthoDB; 293434at2759; -.
DR PhylomeDB; O22854; -.
DR BioCyc; ARA:AT2G43400-MON; -.
DR PRO; PR:O22854; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22854; baseline and differential.
DR Genevisible; O22854; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010230; P:alternative respiration; IMP:TAIR.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0006552; P:leucine catabolic process; IMP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IEP:TAIR.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10617; PTHR10617; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Transit peptide; Transport; Ubiquinone.
FT TRANSIT 1..90
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 91..633
FT /note="Electron transfer flavoprotein-ubiquinone
FT oxidoreductase, mitochondrial"
FT /id="PRO_0000424901"
FT INTRAMEM 140..161
FT /evidence="ECO:0000250"
FT INTRAMEM 401..421
FT /evidence="ECO:0000255"
FT DOMAIN 593..622
FT /note="4Fe-4S ferredoxin-type"
FT BINDING 102..116
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 334
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 578
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 602
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 605
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 608
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 633 AA; 70128 MW; EDDDFAFC43591CB9 CRC64;
MHRFLVKLSS SSSPFSNQLR SLKNQRLILP LLPSSKPFTS SSVSPPPSPL NASNRFGYPY
SADLFRNLSP LNPNSRILGV NGITSSRCIS SEAVRESIEY DVLIVGAGPA GLSAAIRLKQ
LSQEKNIDLS VCVVEKGAEV GGHIISGNVF EPLALDELLP HWRQEHAPIE IPASSDKFWF
LTKDRAFSLP SPFDNKGNYV ISLSQLVRWL GGKAEELGTE IYPGFSASEV LFDASDKVVG
IATKDMGISK DGSKKENFQP GVDIKGRVTL FAEGCRGSLS ERIIKKYKLR EEVNAQHQTY
ALGIKEVWEI DESKHNPGEV IHTLGWPLDP KTYGGSFLYH MNDRQVALGL VVALNYHNPF
LNPYEEFQKL KHHPAIKGIL EGGTVLQYGA RTLNEGGFQS IPYPVFPGGA IIGCSAGFLN
VPKIKGTHTA MKSGMLAAEA AFGALHEGLN MNTYWDNLRD SWVWKELYAA RNYRPAFEYG
LLPGLAISAM EHYVLKGKVP FTLKHGKADH EATDLARKWT PIVYPKPDGV LSFDVPTSLY
RSNTNHDHDQ PSHLRLRDPK IPEKVNFPEY AAPESRYCPA RVYEYIEDEE GKPKLQINAQ
NCLHCKACDI KDPKQNIEWT VPEGGGGPAY SLM
