ID   NDH2_YEAST              Reviewed;         545 AA.
AC   Q07500;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=External NADH-ubiquinone oxidoreductase 2, mitochondrial;
DE            EC=1.6.5.3;
DE   AltName: Full=External NADH dehydrogenase 2;
DE   Flags: Precursor;
GN   Name=NDE2; Synonyms=NDH2; OrderedLocusNames=YDL085W;
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 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
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   [3]
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   [4]
RP   FUNCTION, AND MASS SPECTROMETRY.
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   [5]
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   [6]
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   [7]
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 NDE1, 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       P38206:RFT1; NbExp=1; IntAct=EBI-38178, EBI-15028;
CC       P38988:YHM1; NbExp=1; IntAct=EBI-38178, EBI-24559;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
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DR   EMBL; Z74133; CAA98651.1; -; Genomic_DNA.
DR   PIR; S67621; S67621.
DR   RefSeq; NP_010198.1; -.
DR   DIP; DIP:5023N; -.
DR   IntAct; Q07500; 11.
DR   Ensembl; YDL085W; Saccharomyces cerevisiae.
DR   GeneID; 851474; -.
DR   GenomeReviews; Z71256_GR; YDL085W.
DR   KEGG; sce:YDL085W; -.
DR   NMPDR; fig|4932.3.peg.938; -.
DR   CYGD; YDL085w; -.
DR   SGD; S000002243; NDE2.
DR   HOGENOM; Q07500; -.
DR   OMA; Q07500; SQVKFLP.
DR   BRENDA; 1.6.5.3; 250.
DR   NextBio; 968774; -.
DR   ArrayExpress; Q07500; -.
DR   GermOnline; YDL085W; 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:0019655; P:glucose catabolic process to ethanol; IGI: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; FAD; Flavoprotein; Mitochondrion; NAD;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     21       Mitochondrion (Potential).
FT   CHAIN        22    545       External NADH-ubiquinone oxidoreductase
FT                                2, mitochondrial.
FT                                /FTId=PRO_0000268687.
FT   NP_BIND      99    129       FAD (By similarity).
FT   NP_BIND     260    296       NAD (By similarity).
SQ   SEQUENCE   545 AA;  61659 MW;  291E81D0FC6D3FD7 CRC64;
     MLPRLGFART ARSIHRFKMT QISKPFFHST EVGKPGPQQK LSKSYTAVFK KWFVRGLKLT
     FYTTLAGTLY VSYELYKESN PPKQVPQSTA FANGLKKKEL VILGTGWGAI SLLKKLDTSL
     YNVTVVSPRS FFLFTPLLPS TPVGTIEMKS IVEPVRSIAR RTPGEVHYIE AEALDVDPKA
     KKVMVQSVSE DEYFVSSLSY DYLVVSVGAK TTTFNIPGVY GNANFLKEIE DAQNIRMKLM
     KTIEQASSFP VNDPERKRLL TFVVVGGGPT GVEFAAELQD YINQDLRKWM PDLSKEMKVI
     LIEALPNILN MFDKTLIKYA EDLFARDEID LQVNTAVKVV EPTYIRTLQN GQTNTDIEYG
     MLVWATGNEP IDFSKTLMSR IPEQTNRRGL LINDKLELLG SENSIYAIGD CTAHTGFFPT
     AQVAHQEGEY LAKILDKKLQ IEQLEWDMLN STDETEVSRL QKEVNLRKSK LDKFNYKHMG
     ALAYIGSETA IADLHMGDSS YQLKGMFAFL FWKSAYLAMC LSIRNRILIA MDWTKVYFLG
     RDSSV
//