ETFD_CAEEL
ID ETFD_CAEEL Reviewed; 597 AA.
AC Q11190;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
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 AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE Short=ETF dehydrogenase;
DE AltName: Full=Lethal protein 721;
DE Flags: Precursor;
GN Name=let-721; ORFNames=C05D11.12;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
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DR EMBL; FO080365; CCD63203.1; -; Genomic_DNA.
DR PIR; D88483; D88483.
DR RefSeq; NP_498415.2; NM_066014.6.
DR AlphaFoldDB; Q11190; -.
DR SMR; Q11190; -.
DR BioGRID; 41134; 5.
DR STRING; 6239.C05D11.12.1; -.
DR World-2DPAGE; 0020:Q11190; -.
DR EPD; Q11190; -.
DR PaxDb; Q11190; -.
DR PeptideAtlas; Q11190; -.
DR EnsemblMetazoa; C05D11.12.1; C05D11.12.1; WBGene00002855.
DR GeneID; 175916; -.
DR UCSC; C05D11.12.1; c. elegans.
DR CTD; 175916; -.
DR WormBase; C05D11.12; CE29662; WBGene00002855; let-721.
DR eggNOG; KOG2415; Eukaryota.
DR GeneTree; ENSGT00390000010773; -.
DR HOGENOM; CLU_009667_4_0_1; -.
DR InParanoid; Q11190; -.
DR OMA; GGGWMYH; -.
DR OrthoDB; 293434at2759; -.
DR PhylomeDB; Q11190; -.
DR Reactome; R-CEL-611105; Respiratory electron transport.
DR PRO; PR:Q11190; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002855; Expressed in adult organism and 4 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
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:0022900; P:electron transport chain; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10617; PTHR10617; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..597
FT /note="Electron transfer flavoprotein-ubiquinone
FT oxidoreductase, mitochondrial"
FT /id="PRO_0000008665"
FT INTRAMEM 91..112
FT /evidence="ECO:0000250"
FT INTRAMEM 409..426
FT /evidence="ECO:0000250"
FT DOMAIN 557..586
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 53..67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 285
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 566
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 569
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 572
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 597 AA; 65335 MW; C0FF09F185A017FB CRC64;
MRISGVTLFR VSSQLRNVVN GQWTTTHYTV KDRSTDPRWK DVDLARESDV YDVVIVGGGP
SGLSAAIRLR QLAEKAQKEL RVCVVEKASV IGGHTLSGAV IETRALDELI PNWKELGAPV
YQQVTSESIA ILTESGRIPV PVLPGVPLAN HGNYIVRLGK VVQWLGEQAE AAGVEVWPEI
AASEVLYNED GSVKGIATSD VGIGKDGAPK DGFARGMEFH AKCTIFAEGC RGHLSKQVLD
KFDLRTHAMT YGIGLKELWE IDPAKHRPGY VEHTMGWPLN VDQYGGSFLY HIEDQGQPLV
SVGFVVALDY ANPNLNPYKE FQKYKTHPSI SKQLEGGKRI GYGARALNEG GFQSIPKLHF
PGGCLVGCSA GFLNVAKLKG THNAMKSGMV AAESIFEDIQ QKGEDVQTID PATYDKNIRD
TYVVKELKAT RNIRPSFNTS LGYIGGLIYS GIFYVFGRGI EPWTLGHGKK DNEKLIPVKD
AKEIDYPKPD GKLTFDLLTS VSLTGTNHTE DQPAHLTLKN DQVPLDVNLA VYGGPEARFC
PAGVYEFVPS EADESKKRLQ INAQNCIHCK TCDIKDPQQN INWVTPEGGG GPKYEGM
