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UniProtKB/Swiss-Prot entry P40215


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NDH1_YEAST
Primary accession number P40215
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 62)
Name and origin of the protein
Protein name External NADH-ubiquinone oxidoreductase 1, mitochondrial [Precursor]
Synonyms EC 1.6.5.3
External NADH dehydrogenase 1
Gene name
Name: NDE1
Synonyms: NDH1
OrderedLocusNames: YMR145C
ORFNames: YM9375.14C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan]
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
Nature 387:90-93(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[3]
PROTEIN SEQUENCE OF 476-480, AND FUNCTION.
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
[4]
FUNCTION.
PubMed=9696750 [NCBI, ExPASy, EBI, Israel, Japan]
Small W.C., McAlister-Henn L.;
"Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae.";
J. Bacteriol. 180:4051-4055(1998).
[5]
FUNCTION.
DOI=10.1074/jbc.273.38.24529; PubMed=9733747 [NCBI, ExPASy, EBI, Israel, Japan]
Luttik M.A.H., Overkamp K.M., Koetter P., de Vries S., van Dijken J.P., Pronk J.T.;
"The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH.";
J. Biol. Chem. 273:24529-24534(1998).
[6]
FUNCTION.
DOI=10.1128/JB.182.10.2823-2830.2000; PubMed=10781551 [NCBI, ExPASy, EBI, Israel, Japan]
Overkamp K.M., Bakker B.M., Koetter P., van Tuijl A., de Vries S., van Dijken J.P., Pronk J.T.;
"In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria.";
J. Bacteriol. 182:2823-2830(2000).
[7]
FUNCTION.
DOI=10.1128/MCB.21.24.8483-8489.2001; PubMed=11713283 [NCBI, ExPASy, EBI, Israel, Japan]
Davidson J.F., Schiestl R.H.;
"Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 21:8483-8489(2001).
[8]
FUNCTION.
DOI=10.1074/jbc.M204079200; PubMed=12032156 [NCBI, ExPASy, EBI, Israel, Japan]
Paahlman I.-L., Larsson C., Averet N., Bunoust O., Boubekeur S., Gustafsson L., Rigoulet M.;
"Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae.";
J. Biol. Chem. 277:27991-27995(2002).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
Comments
  • FUNCTION: External NADH dehydrogenase required for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. With NDE2, performes the mitochondrial oxidation of cytosolic NADH under these growth conditions. Regulates the mitochondrial glycerol-3-phosphate dehydrogenase, GUT2, also involved in cytosolic NADH oxydation.
  • CATALYTIC ACTIVITY: NADH + ubiquinone = NAD+ + ubiquinol.
  • INTERACTION:
    P10592:SSA2; NbExp=1; IntAct=EBI-27294, EBI-8603;
  • SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
  • MISCELLANEOUS: Present with 4930 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the NADH dehydrogenase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z47071; CAA87359.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692785; AAT92804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S50401; S50401.
RefSeq NP_013865.1; -.
3D structure databases
ModBase P40215.
Protein-protein interaction databases
DIP DIP:6528N; -.
IntAct P40215; -.
Organism-specific databases
CYGD YMR145c; -.
SGD S000004753; NDE1.
Yeast-GFP YMR145C.
Gene expression databases
ArrayExpress P40215; -.
GermOnline YMR145C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0003954; Molecular function: NADH dehydrogenase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0001300; Biological process: chronological cell aging (inferred from mutant phenotype from SGD).
GO:0019655; Biological process: glucose catabolic process to ethanol (inferred from mutant phenotype from SGD).
GO:0006116; Biological process: NADH oxidation (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
BLOCKS P40215.
Proteomic databases
PeptideAtlas P40215; -.
Genome annotation databases
Ensembl YMR145C; Saccharomyces cerevisiae. [Contig view]
GeneID 855176; -.
GenomeReviews Z71257_GR; YMR145C.
KEGG sce:YMR145C; -.
NMPDR fig|4932.3.peg.4915; -.
Phylogenomic databases
HOGENOM P40215; -.
Other
LinkHub P40215; -.
ProtoNet P40215.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NAD; Oxidoreductase; Transit peptide; Ubiquinone.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    41  41     Mitochondrion (Potential). 
CHAIN   42   560  519     External NADH-ubiquinone oxidoreductase 1, mitochondrial. PRO_0000203306
NP_BIND   114   144  31     FAD (By similarity). 
NP_BIND   275   311  37     NAD (By similarity). 
Sequence information
Length: 560 AA [This is the length of the unprocessed precursor] Molecular weight: 62774 Da [This is the MW of the unprocessed precursor] CRC64: 10B1795E12E29C34 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIRQSLMKTV WANSSRFSLQ SKSGLVKYAK NRSFHAARNL LEDKKVILQK VAPTTGVVAK 

        70         80         90        100        110        120 
QSFFKRTGKF TLKALLYSAL AGTAYVSYSL YREANPSTQV PQSDTFPNGS KRKTLVILGS 

       130        140        150        160        170        180 
GWGSVSLLKN LDTTLYNVVV VSPRNYFLFT PLLPSTPVGT IELKSIVEPV RTIARRSHGE 

       190        200        210        220        230        240 
VHYYEAEAYD VDPENKTIKV KSSAKNNDYD LDLKYDYLVV GVGAQPNTFG TPGVYEYSSF 

       250        260        270        280        290        300 
LKEISDAQEI RLKIMSSIEK AASLSPKDPE RARLLSFVVV GGGPTGVEFA AELRDYVDQD 

       310        320        330        340        350        360 
LRKWMPELSK EIKVTLVEAL PNILNMFDKY LVDYAQDLFK EEKIDLRLKT MVKKVDATTI 

       370        380        390        400        410        420 
TAKTGDGDIE NIPYGVLVWA TGNAPREVSK NLMTKLEEQD SRRGLLIDNK LQLLGAKGSI 

       430        440        450        460        470        480 
FAIGDCTFHP GLFPTAQVAH QEGEYLAQYF KKAYKIDQLN WKMTHAKDDS EVARLKNQIV 

       490        500        510        520        530        540 
KTQSQIEDFK YNHKGALAYI GSDKAIADLA VGEAKYRLAG SFTFLFWKSA YLAMCLSFRN 

       550        560 
RVLVAMDWAK VYFLGRDSSI 

P40215 in FASTA format

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