ID   ETFD_YEAST              Reviewed;         631 AA.
AC   Q08822;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 78.
DE   RecName: Full=Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
DE            Short=ETF-ubiquinone oxidoreductase;
DE            Short=ETF-QO;
DE            EC=1.5.5.1;
DE   AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE            Short=ETF dehydrogenase;
DE   Flags: Precursor;
GN   OrderedLocusNames=YOR356W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313270; PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   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.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21393706; PubMed=11502169; DOI=10.1021/bi010277r;
RA   Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N.,
RA   Manon S., Schmitter J.-M.;
RT   "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT   complex.";
RL   Biochemistry 40:9758-9769(2001).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   MEDLINE=22975177; PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
RA   Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
RA   Rehling P., Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
CC   -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Reduced electron-transferring flavoprotein +
CC       ubiquinone = electron-transferring flavoprotein + ubiquinol.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- INTERACTION:
CC       P36156:ECM4; NbExp=1; IntAct=EBI-6705, EBI-2042717;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- MISCELLANEOUS: Present with 3320 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the ETF-QO/fixC family.
CC   -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.
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DR   EMBL; Z75264; CAA99685.1; -; Genomic_DNA.
DR   PIR; S67268; S67268.
DR   RefSeq; NP_015001.1; -.
DR   DIP; DIP:6685N; -.
DR   IntAct; Q08822; 5.
DR   PeptideAtlas; Q08822; -.
DR   Ensembl; YOR356W; Saccharomyces cerevisiae.
DR   GeneID; 854538; -.
DR   GenomeReviews; Y13140_GR; YOR356W.
DR   KEGG; sce:YOR356W; -.
DR   NMPDR; fig|4932.3.peg.6120; -.
DR   CYGD; YOR356w; -.
DR   SGD; S000005883; YOR356W.
DR   HOGENOM; Q08822; -.
DR   OMA; Q08822; YTPGMEL.
DR   BRENDA; 1.5.5.1; 250.
DR   NextBio; 976937; -.
DR   ArrayExpress; Q08822; -.
DR   GermOnline; YOR356W; Saccharomyces cerevisiae.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004174; F:electron-transferring-flavoprotein dehydrog...; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006116; P:NADH oxidation; IPI:SGD.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR007859; ETFD_OxRdtase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   Pfam; PF05187; ETF_QO; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Electron transport; FAD; Flavoprotein;
KW   Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Transit peptide;
KW   Transport; Ubiquinone.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    631       Probable electron transfer flavoprotein-
FT                                ubiquinone oxidoreductase, mitochondrial.
FT                                /FTId=PRO_0000008667.
FT   DOMAIN      591    620       4Fe-4S ferredoxin-type.
FT   NP_BIND      65     79       FAD (Potential).
FT   METAL       574    574       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       600    600       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       603    603       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       606    606       Iron-sulfur (4Fe-4S) (Potential).
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
//