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Reviewed, UniProtKB/Swiss-Prot Q07500 (NDH2_YEAST)

Last modified January 19, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    External NADH-ubiquinone oxidoreductase 2, mitochondrial
    EC=1.6.5.3
Alternative name(s):
    External NADH dehydrogenase 2
Gene names
Name: NDE2
Synonyms: NDH2
Ordered Locus Names: YDL085W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

External NADH dehydrogenase required for optimum cellular growth with a number of nonfermentable carbon sources, including ethanol. With NDE1, 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. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6

Catalytic activity

NADH + ubiquinone = NAD+ + ubiquinol.

Subcellular location

Mitochondrion intermembrane space Ref.7.

Sequence similarities

Belongs to the NADH dehydrogenase family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

RFT1P382061EBI-38178,EBI-15028
YHM1P389881EBI-38178,EBI-24559

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion Potential
Chain22 – 545524External NADH-ubiquinone oxidoreductase 2, mitochondrial
PRO_0000268687

Regions

Nucleotide binding99 – 12931FAD By similarity
Nucleotide binding260 – 29637NAD By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q07500-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 291E81D0FC6D3FD7

FASTA54561,659
        10         20         30         40         50         60 
MLPRLGFART ARSIHRFKMT QISKPFFHST EVGKPGPQQK LSKSYTAVFK KWFVRGLKLT 

        70         80         90        100        110        120 
FYTTLAGTLY VSYELYKESN PPKQVPQSTA FANGLKKKEL VILGTGWGAI SLLKKLDTSL 

       130        140        150        160        170        180 
YNVTVVSPRS FFLFTPLLPS TPVGTIEMKS IVEPVRSIAR RTPGEVHYIE AEALDVDPKA 

       190        200        210        220        230        240 
KKVMVQSVSE DEYFVSSLSY DYLVVSVGAK TTTFNIPGVY GNANFLKEIE DAQNIRMKLM 

       250        260        270        280        290        300 
KTIEQASSFP VNDPERKRLL TFVVVGGGPT GVEFAAELQD YINQDLRKWM PDLSKEMKVI 

       310        320        330        340        350        360 
LIEALPNILN MFDKTLIKYA EDLFARDEID LQVNTAVKVV EPTYIRTLQN GQTNTDIEYG 

       370        380        390        400        410        420 
MLVWATGNEP IDFSKTLMSR IPEQTNRRGL LINDKLELLG SENSIYAIGD CTAHTGFFPT 

       430        440        450        460        470        480 
AQVAHQEGEY LAKILDKKLQ IEQLEWDMLN STDETEVSRL QKEVNLRKSK LDKFNYKHMG 

       490        500        510        520        530        540 
ALAYIGSETA IADLHMGDSS YQLKGMFAFL FWKSAYLAMC LSIRNRILIA MDWTKVYFLG 


RDSSV

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References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH."
Luttik M.A.H., Overkamp K.M., Koetter P., de Vries S., van Dijken J.P., Pronk J.T.
J. Biol. Chem. 273:24529-24534(1998) [PubMed: 9733747] [Abstract]
Cited for: FUNCTION.
[3]"In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria."
Overkamp K.M., Bakker B.M., Koetter P., van Tuijl A., de Vries S., van Dijken J.P., Pronk J.T.
J. Bacteriol. 182:2823-2830(2000) [PubMed: 10781551] [Abstract]
Cited for: FUNCTION.
[4]"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
Biochemistry 40:9758-9769(2001) [PubMed: 11502169] [Abstract]
Cited for: FUNCTION, MASS SPECTROMETRY.
[5]"Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in Saccharomyces cerevisiae."
Davidson J.F., Schiestl R.H.
Mol. Cell. Biol. 21:8483-8489(2001) [PubMed: 11713283] [Abstract]
Cited for: FUNCTION.
[6]"Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae."
Paahlman I.-L., Larsson C., Averet N., Bunoust O., Boubekeur S., Gustafsson L., Rigoulet M.
J. Biol. Chem. 277:27991-27995(2002) [PubMed: 12032156] [Abstract]
Cited for: FUNCTION.
[7]"The proteome of Saccharomyces cerevisiae mitochondria."
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.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z74133 Genomic DNA. Translation: CAA98651.1.
PIRS67621.
RefSeqNP_010198.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5023N.
IntActQ07500. 11 interactions.
STRINGQ07500.

Proteomic databases

PRIDEQ07500.

Genome annotation databases

EnsemblYDL085W; YDL085W; YDL085W; Saccharomyces cerevisiae. [Genome view]
GeneID851474.
KEGGsce:YDL085W.
NMPDRfig|4932.3.peg.938.

Organism-specific databases

CYGDYDL085w.
SGDS000002243. NDE2.

Phylogenomic databases

eggNOGfuNOG04442.
HOGENOMHBG319217.
OMASPRNYFT.
OrthoDBEOG9Q2FZS.
PhylomeDBQ07500.

Enzyme and pathway databases

BRENDA1.6.5.3. 250.

Gene expression databases

ArrayExpressQ07500.
GenevestigatorQ07500.
GermOnlineYDL085W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio968774.

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Entry information

Entry nameNDH2_YEAST
AccessionPrimary (citable) accession number: Q07500
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents