ID   NDH1_YEAST              Reviewed;         560 AA.
AC   P40215;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 64.
DE   RecName: Full=External NADH-ubiquinone oxidoreductase 1, mitochondrial;
DE            EC=1.6.5.3;
DE   AltName: Full=External NADH dehydrogenase 1;
DE   Flags: Precursor;
GN   Name=NDE1; Synonyms=NDH1; OrderedLocusNames=YMR145C;
GN   ORFNames=YM9375.14C;
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 204511 / S288c / AB972;
RX   MEDLINE=97313268; PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [3]
RP   PROTEIN SEQUENCE OF 476-480, AND FUNCTION.
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   [4]
RP   FUNCTION.
RX   PubMed=9696750;
RA   Small W.C., McAlister-Henn L.;
RT   "Identification of a cytosolically directed NADH dehydrogenase in
RT   mitochondria of Saccharomyces cerevisiae.";
RL   J. Bacteriol. 180:4051-4055(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=9733747; DOI=10.1074/jbc.273.38.24529;
RA   Luttik M.A.H., Overkamp K.M., Koetter P., de Vries S.,
RA   van Dijken J.P., Pronk J.T.;
RT   "The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate
RT   mitochondrial NADH dehydrogenases catalyzing the oxidation of
RT   cytosolic NADH.";
RL   J. Biol. Chem. 273:24529-24534(1998).
RN   [6]
RP   FUNCTION.
RX   PubMed=10781551; DOI=10.1128/JB.182.10.2823-2830.2000;
RA   Overkamp K.M., Bakker B.M., Koetter P., van Tuijl A., de Vries S.,
RA   van Dijken J.P., Pronk J.T.;
RT   "In vivo analysis of the mechanisms for oxidation of cytosolic NADH by
RT   Saccharomyces cerevisiae mitochondria.";
RL   J. Bacteriol. 182:2823-2830(2000).
RN   [7]
RP   FUNCTION.
RX   PubMed=11713283; DOI=10.1128/MCB.21.24.8483-8489.2001;
RA   Davidson J.F., Schiestl R.H.;
RT   "Mitochondrial respiratory electron carriers are involved in oxidative
RT   stress during heat stress in Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 21:8483-8489(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=12032156; DOI=10.1074/jbc.M204079200;
RA   Paahlman I.-L., Larsson C., Averet N., Bunoust O., Boubekeur S.,
RA   Gustafsson L., Rigoulet M.;
RT   "Kinetic regulation of the mitochondrial glycerol-3-phosphate
RT   dehydrogenase by the external NADH dehydrogenase in Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 277:27991-27995(2002).
RN   [9]
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   [10]
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: External NADH dehydrogenase required for optimum
CC       cellular growth with a number of nonfermentable carbon sources,
CC       including ethanol. With NDE2, performes the mitochondrial
CC       oxidation of cytosolic NADH under these growth conditions.
CC       Regulates the mitochondrial glycerol-3-phosphate dehydrogenase,
CC       GUT2, also involved in cytosolic NADH oxydation.
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol.
CC   -!- INTERACTION:
CC       P10592:SSA2; NbExp=1; IntAct=EBI-27294, EBI-8603;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC   -!- MISCELLANEOUS: Present with 4930 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
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DR   EMBL; Z47071; CAA87359.1; -; Genomic_DNA.
DR   EMBL; AY692785; AAT92804.1; -; Genomic_DNA.
DR   PIR; S50401; S50401.
DR   RefSeq; NP_013865.1; -.
DR   DIP; DIP:6528N; -.
DR   IntAct; P40215; -.
DR   PeptideAtlas; P40215; -.
DR   Ensembl; YMR145C; Saccharomyces cerevisiae.
DR   GeneID; 855176; -.
DR   GenomeReviews; Z71257_GR; YMR145C.
DR   KEGG; sce:YMR145C; -.
DR   NMPDR; fig|4932.3.peg.4915; -.
DR   CYGD; YMR145c; -.
DR   SGD; S000004753; NDE1.
DR   HOGENOM; P40215; -.
DR   LinkHub; P40215; -.
DR   NextBio; 978623; -.
DR   ArrayExpress; P40215; -.
DR   GermOnline; YMR145C; Saccharomyces cerevisiae.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0001300; P:chronological cell aging; IMP:SGD.
DR   GO; GO:0019655; P:glucose catabolic process to ethanol; IMP:SGD.
DR   GO; GO:0006116; P:NADH oxidation; IDA:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; FAD; Flavoprotein;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide; Ubiquinone.
FT   TRANSIT       1     41       Mitochondrion (Potential).
FT   CHAIN        42    560       External NADH-ubiquinone oxidoreductase
FT                                1, mitochondrial.
FT                                /FTId=PRO_0000203306.
FT   NP_BIND     114    144       FAD (By similarity).
FT   NP_BIND     275    311       NAD (By similarity).
SQ   SEQUENCE   560 AA;  62774 MW;  10B1795E12E29C34 CRC64;
     MIRQSLMKTV WANSSRFSLQ SKSGLVKYAK NRSFHAARNL LEDKKVILQK VAPTTGVVAK
     QSFFKRTGKF TLKALLYSAL AGTAYVSYSL YREANPSTQV PQSDTFPNGS KRKTLVILGS
     GWGSVSLLKN LDTTLYNVVV VSPRNYFLFT PLLPSTPVGT IELKSIVEPV RTIARRSHGE
     VHYYEAEAYD VDPENKTIKV KSSAKNNDYD LDLKYDYLVV GVGAQPNTFG TPGVYEYSSF
     LKEISDAQEI RLKIMSSIEK AASLSPKDPE RARLLSFVVV GGGPTGVEFA AELRDYVDQD
     LRKWMPELSK EIKVTLVEAL PNILNMFDKY LVDYAQDLFK EEKIDLRLKT MVKKVDATTI
     TAKTGDGDIE NIPYGVLVWA TGNAPREVSK NLMTKLEEQD SRRGLLIDNK LQLLGAKGSI
     FAIGDCTFHP GLFPTAQVAH QEGEYLAQYF KKAYKIDQLN WKMTHAKDDS EVARLKNQIV
     KTQSQIEDFK YNHKGALAYI GSDKAIADLA VGEAKYRLAG SFTFLFWKSA YLAMCLSFRN
     RVLVAMDWAK VYFLGRDSSI
//