NDH1_YEAST
ID NDH1_YEAST Reviewed; 560 AA.
AC P40215; D6VZW7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=External NADH-ubiquinone oxidoreductase 1, mitochondrial;
DE EC=1.6.5.9;
DE AltName: Full=External NADH dehydrogenase 1;
DE Flags: Precursor;
GN Name=NDE1; Synonyms=NDH1; OrderedLocusNames=YMR145C; ORFNames=YM9375.14C;
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=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., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 476-480, AND FUNCTION.
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 [5]
RP FUNCTION.
RX PubMed=9696750; DOI=10.1128/jb.180.16.4051-4055.1998;
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 NDE2, 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:9696750,
CC 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 -!- MISCELLANEOUS: Present with 4930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family. {ECO:0000305}.
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DR EMBL; Z47071; CAA87359.1; -; Genomic_DNA.
DR EMBL; AY692785; AAT92804.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10041.1; -; Genomic_DNA.
DR PIR; S50401; S50401.
DR RefSeq; NP_013865.1; NM_001182647.1.
DR AlphaFoldDB; P40215; -.
DR SMR; P40215; -.
DR BioGRID; 35321; 121.
DR DIP; DIP-6528N; -.
DR IntAct; P40215; 7.
DR STRING; 4932.YMR145C; -.
DR MaxQB; P40215; -.
DR PaxDb; P40215; -.
DR PRIDE; P40215; -.
DR EnsemblFungi; YMR145C_mRNA; YMR145C; YMR145C.
DR GeneID; 855176; -.
DR KEGG; sce:YMR145C; -.
DR SGD; S000004753; NDE1.
DR VEuPathDB; FungiDB:YMR145C; -.
DR eggNOG; KOG2495; Eukaryota.
DR GeneTree; ENSGT00940000176602; -.
DR HOGENOM; CLU_021377_1_0_1; -.
DR InParanoid; P40215; -.
DR OMA; VDPRSYM; -.
DR BioCyc; MetaCyc:G3O-32837-MON; -.
DR BioCyc; YEAST:G3O-32837-MON; -.
DR SABIO-RK; P40215; -.
DR PRO; PR:P40215; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40215; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0019655; P:glycolytic fermentation to ethanol; IMP:SGD.
DR GO; GO:0006116; P:NADH oxidation; IDA:SGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP: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 Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NAD;
KW Oxidoreductase; Reference proteome; Transit peptide; Ubiquinone.
FT TRANSIT 1..41
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 42..560
FT /note="External NADH-ubiquinone oxidoreductase 1,
FT mitochondrial"
FT /id="PRO_0000203306"
FT BINDING 114..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 275..311
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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
