ETFD_YEAST
ID ETFD_YEAST Reviewed; 631 AA.
AC Q08822; D6W351;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
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=Changed intracellular redox state protein 2;
DE AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE Short=ETF dehydrogenase;
DE Flags: Precursor;
GN Name=CIR2; OrderedLocusNames=YOR356W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=21253464; DOI=10.2174/1874285801004010075;
RA Lopes J., Pinto M.J., Rodrigues A., Vasconcelos F., Oliveira R.;
RT "The Saccharomyces cerevisiae genes, AIM45, YGR207c/CIR1 and YOR356w/CIR2,
RT are involved in cellular redox state under stress conditions.";
RL Open Microbiol. J. 4:75-82(2010).
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
CC {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278}.
CC -!- DISRUPTION PHENOTYPE: Displays higher growth rate and higher
CC sensitivity to superoxide and heat stress, on nonfermentable carbon
CC sources. Leads to decreased intracellular oxidation upon heat shock.
CC {ECO:0000269|PubMed:21253464}.
CC -!- MISCELLANEOUS: Present with 3320 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
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DR EMBL; Z75264; CAA99685.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11117.1; -; Genomic_DNA.
DR PIR; S67268; S67268.
DR RefSeq; NP_015001.1; NM_001183776.1.
DR AlphaFoldDB; Q08822; -.
DR SMR; Q08822; -.
DR BioGRID; 34741; 69.
DR DIP; DIP-6685N; -.
DR IntAct; Q08822; 2.
DR STRING; 4932.YOR356W; -.
DR iPTMnet; Q08822; -.
DR MaxQB; Q08822; -.
DR PaxDb; Q08822; -.
DR PRIDE; Q08822; -.
DR EnsemblFungi; YOR356W_mRNA; YOR356W; YOR356W.
DR GeneID; 854538; -.
DR KEGG; sce:YOR356W; -.
DR SGD; S000005883; CIR2.
DR VEuPathDB; FungiDB:YOR356W; -.
DR eggNOG; KOG2415; Eukaryota.
DR GeneTree; ENSGT00390000010773; -.
DR HOGENOM; CLU_009667_4_0_1; -.
DR InParanoid; Q08822; -.
DR OMA; GGGWMYH; -.
DR BioCyc; YEAST:G3O-33827-MON; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR PRO; PR:Q08822; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08822; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
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 1: Evidence at protein 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..631
FT /note="Probable electron transfer flavoprotein-ubiquinone
FT oxidoreductase, mitochondrial"
FT /id="PRO_0000008667"
FT DOMAIN 591..620
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 65..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 574
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 600
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 603
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 606
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 631 AA; 69634 MW; 7493F67093D88391 CRC64;
MIKFTNENLI RGIRMTISAK SRHLALGTDM TRKFSLSCRF LNKANLTEEE KELLNEPRAR
DYVDVCIVGG GPAGLATAIK LKQLDNSSGT GQLRVVVLEK SSVLGGQTVS GAILEPGVWK
ELFPDEKSDI GIPLPKELAT LVTKEHLKFL KGKWAISVPE PSQMINKGRN YIVSLNQVVG
YLGEKAEEVG VEVYPGIAVS DLIYDENNAV KGVITKDAGI SKSGKPKETF ERGMEFWARQ
TVLAEGCHGS LTKQALAKYD LRKGRQHQTY GLGIKEVWEV KPENFNKGFA AHTMGYPLTN
DVYGGGFQYH FGDGLVTVGL VVGLDYKNPY VSPYKEFQKM KHHPYYSKVL EGGKCIAYAA
RALNEGGLQS VPKLNFPGGV LVGASAGFMN VPKIKGTHTA MKSGLLAAES IFESIKGLPV
LEEVEDEDAK MAMFDKEATI NLESYESAFK ESSIYKELYE VRNIRPSFSG KLGGYGGMIY
SGIDSLILKG KVPWTLKFDE KNDGEILEPA SKYKPIEYPK PDGVISFDIL TSVSRTGTYH
DDDEPCHLRV PGQDMVKYAE RSFPVWKGVE SRFCPAGVYE FVKDEKSPVG TRLQINSQNC
IHCKTCDIKA PRQDITWKVP EGGDGPKYTL T
