ETFD_SCHPO
ID ETFD_SCHPO Reviewed; 632 AA.
AC P87111;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable 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 Flags: Precursor;
GN ORFNames=SPAC20G8.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB08598.1; -; Genomic_DNA.
DR PIR; T38126; T38126.
DR RefSeq; NP_593321.1; NM_001018752.2.
DR AlphaFoldDB; P87111; -.
DR SMR; P87111; -.
DR BioGRID; 278470; 6.
DR STRING; 4896.SPAC20G8.04c.1; -.
DR iPTMnet; P87111; -.
DR MaxQB; P87111; -.
DR PaxDb; P87111; -.
DR PRIDE; P87111; -.
DR EnsemblFungi; SPAC20G8.04c.1; SPAC20G8.04c.1:pep; SPAC20G8.04c.
DR GeneID; 2541985; -.
DR KEGG; spo:SPAC20G8.04c; -.
DR PomBase; SPAC20G8.04c; -.
DR VEuPathDB; FungiDB:SPAC20G8.04c; -.
DR eggNOG; KOG2415; Eukaryota.
DR HOGENOM; CLU_009667_4_0_1; -.
DR InParanoid; P87111; -.
DR OMA; GGGWMYH; -.
DR PhylomeDB; P87111; -.
DR Reactome; R-SPO-611105; Respiratory electron transport.
DR PRO; PR:P87111; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISM:PomBase.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0006116; P:NADH oxidation; ISO:PomBase.
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 ?..632
FT /note="Probable electron transfer flavoprotein-ubiquinone
FT oxidoreductase, mitochondrial"
FT /id="PRO_0000008666"
FT DOMAIN 592..621
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 93..107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 575
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 601
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 604
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 607
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 632 AA; 69472 MW; 1B0F22374E33771B CRC64;
MSYLSRSALA RSVGAKHLTG VLRKIGRRGG RSMHVLPLAS PSTLLKISSQ TLRQDFTVLG
ARNFHSSSVR LNELTDNLRK LDTIEREVED VDVCIVGAGP AGLSAAIRIK QQAAKANRDI
RVVVLEKAAE PGNHSVSGAV IQPTALDELL PNWRDDPPEN CTAVTHDKMK FLIPKLHFPI
PVPPAMKNHG NYVMSLAEFT RWLAAKAEEY GVEIYPSFAA SEVLYNKDGS VIGVATNDFG
VDSKGLPKDN FERGMAFHAP VTLFAEGAHG SLSKSIIKRF NLRGNCEPQT YGLGVKEVWR
VPDENFRKGE VAHTLGWPMR NDTYGGGFMY QFGDNYVTVG LVVGLDYPNP YVSPALEFQR
MKQNPFFAKV LKGGKCLEYA ARALNEGGYQ AIPKLVFPGG ALIGCSAGFV NVAKIKGTHT
AMKSGIVAAD AIVDAFGRDA ASKPLLLNDY EENLKNTYVF KELYSVRNIR PSFHSFLGNY
GGMAYSAVEA YVLKGRVPWT LKHKGGDAKA TKSASKYKPI NYPKPDNVLS FDIPTSVSRS
ATMHAENQPC HLFDHRPKDR KSCFETYKGV ENKFCPAGVY EYVNDEASSY GKRFVINSQN
CVHCKTCDIK DPLQGIQWKT PQGGDGPKYT LT
