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Protein

External NADH-ubiquinone oxidoreductase 2, mitochondrial

Gene

NDE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 oxidation.5 Publications

Catalytic activityi

NADH + ubiquinone = NAD+ + ubiquinol.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi99 – 12931FADBy similarityAdd
BLAST
Nucleotide bindingi260 – 29637NADBy similarityAdd
BLAST

GO - Molecular functioni

  • NADH dehydrogenase activity Source: SGD

GO - Biological processi

  • glycolytic fermentation to ethanol Source: SGD
  • NADH oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NAD

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29494-MONOMER.
YEAST:G3O-29494-MONOMER.
SABIO-RKQ07500.

Names & Taxonomyi

Protein namesi
Recommended name:
External NADH-ubiquinone oxidoreductase 2, mitochondrial (EC:1.6.5.9)
Alternative name(s):
External NADH dehydrogenase 2
Gene namesi
Name:NDE2
Synonyms:NDH2
Ordered Locus Names:YDL085W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL085W.
SGDiS000002243. NDE2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial intermembrane space Source: UniProtKB-SubCell
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121MitochondrionSequence analysisAdd
BLAST
Chaini22 – 545524External NADH-ubiquinone oxidoreductase 2, mitochondrialPRO_0000268687Add
BLAST

PTM databases

iPTMnetiQ07500.

Interactioni

Protein-protein interaction databases

BioGridi31976. 44 interactions.
DIPiDIP-5023N.
IntActiQ07500. 4 interactions.
MINTiMINT-494556.

Structurei

3D structure databases

ProteinModelPortaliQ07500.
SMRiQ07500. Positions 97-542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NADH dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000065152.
HOGENOMiHOG000182501.
InParanoidiQ07500.
KOiK17871.
OMAiVEHAMAI.
OrthoDBiEOG7034S6.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07500-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPRLGFART ARSIHRFKMT QISKPFFHST EVGKPGPQQK LSKSYTAVFK
60 70 80 90 100
KWFVRGLKLT FYTTLAGTLY VSYELYKESN PPKQVPQSTA FANGLKKKEL
110 120 130 140 150
VILGTGWGAI SLLKKLDTSL YNVTVVSPRS FFLFTPLLPS TPVGTIEMKS
160 170 180 190 200
IVEPVRSIAR RTPGEVHYIE AEALDVDPKA KKVMVQSVSE DEYFVSSLSY
210 220 230 240 250
DYLVVSVGAK TTTFNIPGVY GNANFLKEIE DAQNIRMKLM KTIEQASSFP
260 270 280 290 300
VNDPERKRLL TFVVVGGGPT GVEFAAELQD YINQDLRKWM PDLSKEMKVI
310 320 330 340 350
LIEALPNILN MFDKTLIKYA EDLFARDEID LQVNTAVKVV EPTYIRTLQN
360 370 380 390 400
GQTNTDIEYG MLVWATGNEP IDFSKTLMSR IPEQTNRRGL LINDKLELLG
410 420 430 440 450
SENSIYAIGD CTAHTGFFPT AQVAHQEGEY LAKILDKKLQ IEQLEWDMLN
460 470 480 490 500
STDETEVSRL QKEVNLRKSK LDKFNYKHMG ALAYIGSETA IADLHMGDSS
510 520 530 540
YQLKGMFAFL FWKSAYLAMC LSIRNRILIA MDWTKVYFLG RDSSV
Length:545
Mass (Da):61,659
Last modified:November 1, 1996 - v1
Checksum:i291E81D0FC6D3FD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74133 Genomic DNA. Translation: CAA98651.1.
BK006938 Genomic DNA. Translation: DAA11774.1.
PIRiS67621.
RefSeqiNP_010198.1. NM_001180144.1.

Genome annotation databases

EnsemblFungiiYDL085W; YDL085W; YDL085W.
GeneIDi851474.
KEGGisce:YDL085W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74133 Genomic DNA. Translation: CAA98651.1.
BK006938 Genomic DNA. Translation: DAA11774.1.
PIRiS67621.
RefSeqiNP_010198.1. NM_001180144.1.

3D structure databases

ProteinModelPortaliQ07500.
SMRiQ07500. Positions 97-542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31976. 44 interactions.
DIPiDIP-5023N.
IntActiQ07500. 4 interactions.
MINTiMINT-494556.

PTM databases

iPTMnetiQ07500.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL085W; YDL085W; YDL085W.
GeneIDi851474.
KEGGisce:YDL085W.

Organism-specific databases

EuPathDBiFungiDB:YDL085W.
SGDiS000002243. NDE2.

Phylogenomic databases

GeneTreeiENSGT00530000065152.
HOGENOMiHOG000182501.
InParanoidiQ07500.
KOiK17871.
OMAiVEHAMAI.
OrthoDBiEOG7034S6.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29494-MONOMER.
YEAST:G3O-29494-MONOMER.
SABIO-RKQ07500.

Miscellaneous databases

PROiQ07500.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiNDH2_YEAST
AccessioniPrimary (citable) accession number: Q07500
Secondary accession number(s): D6VRR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.