NDH2_YEAST
ID NDH2_YEAST Reviewed; 545 AA.
AC Q07500; D6VRR4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=External NADH-ubiquinone oxidoreductase 2, mitochondrial;
DE EC=1.6.5.9;
DE AltName: Full=External NADH dehydrogenase 2;
DE Flags: Precursor;
GN Name=NDE2; Synonyms=NDH2; OrderedLocusNames=YDL085W;
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=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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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 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 FUNCTION.
RX PubMed=9733747; DOI=10.1074/jbc.273.38.24529;
RA Luttik M.A.H., Overkamp K.M., Koetter P., de Vries S., van Dijken J.P.,
RA Pronk J.T.;
RT "The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate
RT mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic
RT NADH.";
RL J. Biol. Chem. 273:24529-24534(1998).
RN [4]
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 [5]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [6]
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 [7]
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 dehydrogenase
RT by the external NADH dehydrogenase in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 277:27991-27995(2002).
RN [8]
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).
CC -!- FUNCTION: External NADH dehydrogenase required for optimum cellular
CC growth with a number of nonfermentable carbon sources, including
CC ethanol. With NDE1, performes the mitochondrial oxidation of cytosolic
CC NADH under these growth conditions. Regulates the mitochondrial
CC glycerol-3-phosphate dehydrogenase, GUT2, also involved in cytosolic
CC NADH oxidation. {ECO:0000269|PubMed:10781551,
CC ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11713283,
CC ECO:0000269|PubMed:12032156, ECO:0000269|PubMed:9733747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + NADH = a ubiquinol + NAD(+);
CC Xref=Rhea:RHEA:23152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:14576278}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; Z74133; CAA98651.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11774.1; -; Genomic_DNA.
DR PIR; S67621; S67621.
DR RefSeq; NP_010198.1; NM_001180144.1.
DR AlphaFoldDB; Q07500; -.
DR SMR; Q07500; -.
DR BioGRID; 31976; 96.
DR DIP; DIP-5023N; -.
DR IntAct; Q07500; 6.
DR MINT; Q07500; -.
DR STRING; 4932.YDL085W; -.
DR iPTMnet; Q07500; -.
DR PaxDb; Q07500; -.
DR PRIDE; Q07500; -.
DR EnsemblFungi; YDL085W_mRNA; YDL085W; YDL085W.
DR GeneID; 851474; -.
DR KEGG; sce:YDL085W; -.
DR SGD; S000002243; NDE2.
DR VEuPathDB; FungiDB:YDL085W; -.
DR eggNOG; KOG2495; Eukaryota.
DR GeneTree; ENSGT00940000176602; -.
DR HOGENOM; CLU_021377_1_0_1; -.
DR InParanoid; Q07500; -.
DR OMA; RGIFQYR; -.
DR BioCyc; MetaCyc:G3O-29494-MON; -.
DR BioCyc; YEAST:G3O-29494-MON; -.
DR SABIO-RK; Q07500; -.
DR PRO; PR:Q07500; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07500; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISS:SGD.
DR GO; GO:0019655; P:glycolytic fermentation to ethanol; IMP:SGD.
DR GO; GO:0006116; P:NADH oxidation; IDA:SGD.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; PTHR43706; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..545
FT /note="External NADH-ubiquinone oxidoreductase 2,
FT mitochondrial"
FT /id="PRO_0000268687"
FT BINDING 99..129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 260..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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
