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Identification
NameExternal NADH-ubiquinone oxidoreductase 2, mitochondrial
Synonyms
  • External NADH dehydrogenase 2
Gene NameNDE2
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionExternal 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
Cellular LocationMitochondrion intermembrane space
SMPDB Pathways
Oxidative phosphorylationPW002461 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Oxidative phosphorylationec00190 Map00190
SMPDB ReactionsNot Available
KEGG Reactions
NADH + Ubiquinone-6 + hydronNAD + Ubiquinol-6
Metabolites
YMDB IDNameView
YMDB00088Ubiquinone Q1Show
YMDB00110NADShow
YMDB00143NADHShow
YMDB00412NAD(+)Show
YMDB00660Ubiquinone-6Show
YMDB00862hydronShow
YMDB00915Ubiquinol-6Show
GO Classification
Component
Not Available
Function
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
FAD or FADH2 binding
oxidoreductase activity
catalytic activity
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 4
LocusYDL085W
Gene Sequence>1638 bp ATGCTGCCCAGACTTGGTTTTGCGAGGACTGCTAGGTCCATACACCGTTTCAAGATGACC CAGATCTCTAAACCTTTTTTCCATTCCACTGAAGTTGGTAAGCCCGGACCACAGCAGAAG CTATCGAAATCTTACACTGCGGTATTCAAGAAATGGTTTGTCAGAGGTTTAAAGTTAACC TTTTACACGACGTTGGCCGGCACATTGTATGTGTCATACGAGCTGTACAAAGAATCGAAC CCACCCAAACAGGTTCCCCAATCGACCGCTTTTGCTAATGGTTTGAAAAAGAAGGAGCTG GTTATTTTGGGTACAGGCTGGGGCGCCATATCTCTTTTGAAGAAATTAGACACGTCTTTG TATAACGTGACCGTGGTGTCGCCAAGAAGCTTCTTTTTGTTCACACCGTTATTACCCTCA ACGCCTGTGGGTACGATAGAGATGAAGTCTATTGTCGAACCGGTTAGATCGATCGCTAGA AGAACGCCTGGAGAAGTTCACTACATTGAGGCGGAAGCGTTGGACGTTGATCCAAAGGCC AAAAAAGTAATGGTGCAATCGGTGTCAGAGGACGAATATTTCGTTTCGAGCTTAAGTTAC GATTATCTTGTTGTTAGTGTAGGCGCTAAAACCACTACTTTTAACATTCCCGGGGTCTAT GGCAATGCTAACTTCTTGAAAGAGATTGAAGATGCTCAAAATATTCGTATGAAGTTAATG AAAACCATAGAACAGGCAAGTTCATTTCCTGTGAACGATCCGGAAAGGAAGCGATTATTA ACGTTCGTGGTTGTTGGAGGGGGCCCTACGGGGGTTGAATTTGCCGCCGAACTGCAAGAT TACATCAATCAAGATTTGAGGAAGTGGATGCCCGACTTAAGTAAAGAAATGAAGGTTATC TTAATTGAAGCCCTGCCTAATATCCTAAACATGTTCGATAAGACGTTGATCAAGTATGCC GAGGACCTTTTTGCCAGAGATGAAATTGACTTGCAAGTGAATACTGCCGTGAAAGTCGTA GAGCCAACCTATATACGCACTCTGCAAAACGGCCAAACAAACACGGATATCGAATACGGG ATGCTGGTTTGGGCCACGGGAAATGAACCAATCGATTTTTCAAAGACACTGATGAGTAGA ATACCGGAGCAAACTAATAGGCGTGGTCTGTTAATTAATGACAAGTTGGAGCTTCTCGGT TCTGAGAATTCGATTTATGCAATTGGTGATTGTACCGCACACACGGGTTTCTTTCCCACG GCACAAGTTGCACATCAGGAAGGCGAATACTTGGCCAAGATCTTGGATAAAAAATTACAG ATAGAACAATTGGAATGGGACATGCTCAACAGTACCGATGAAACTGAGGTATCACGTCTA CAAAAAGAGGTTAATTTGAGGAAATCTAAGTTGGATAAGTTCAACTACAAGCATATGGGT GCCCTTGCGTACATCGGCTCTGAAACCGCAATTGCAGATTTGCATATGGGCGACTCATCA TACCAGTTGAAAGGTATGTTTGCCTTCTTGTTTTGGAAATCCGCTTATTTGGCCATGTGT CTCTCTATCAGGAATAGGATTTTAATTGCCATGGACTGGACCAAAGTTTACTTTCTTGGA AGGGATTCCTCCGTGTAG
Protein Properties
Pfam Domain Function
Protein Residues545
Protein Molecular Weight61658.69922
Protein Theoretical pI9.07
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>External NADH-ubiquinone oxidoreductase 2, mitochondrial MLPRLGFARTARSIHRFKMTQISKPFFHSTEVGKPGPQQKLSKSYTAVFKKWFVRGLKLT FYTTLAGTLYVSYELYKESNPPKQVPQSTAFANGLKKKELVILGTGWGAISLLKKLDTSL YNVTVVSPRSFFLFTPLLPSTPVGTIEMKSIVEPVRSIARRTPGEVHYIEAEALDVDPKA KKVMVQSVSEDEYFVSSLSYDYLVVSVGAKTTTFNIPGVYGNANFLKEIEDAQNIRMKLM KTIEQASSFPVNDPERKRLLTFVVVGGGPTGVEFAAELQDYINQDLRKWMPDLSKEMKVI LIEALPNILNMFDKTLIKYAEDLFARDEIDLQVNTAVKVVEPTYIRTLQNGQTNTDIEYG MLVWATGNEPIDFSKTLMSRIPEQTNRRGLLINDKLELLGSENSIYAIGDCTAHTGFFPT AQVAHQEGEYLAKILDKKLQIEQLEWDMLNSTDETEVSRLQKEVNLRKSKLDKFNYKHMG ALAYIGSETAIADLHMGDSSYQLKGMFAFLFWKSAYLAMCLSIRNRILIAMDWTKVYFLG RDSSV
References
External Links
ResourceLink
Saccharomyces Genome Database NDE2
Uniprot IDQ07500
Uniprot NameNDH2_YEAST
GenBank Gene IDZ74133
Genebank Protein ID1431110
General Reference
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, 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., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Luttik, M. A., Overkamp, K. M., Kotter, P., de Vries, S., van Dijken, J. P., Pronk, J. T. (1998). "The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH." J Biol Chem 273:24529-24534.9733747
  • Overkamp, K. M., Bakker, B. M., Kotter, P., van Tuijl, A., de Vries, S., van Dijken, J. P., Pronk, J. T. (2000). "In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria." J Bacteriol 182:2823-2830.10781551
  • Grandier-Vazeille, X., Bathany, K., Chaignepain, S., Camougrand, N., Manon, S., Schmitter, J. M. (2001). "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Biochemistry 40:9758-9769.11502169
  • Davidson, J. F., Schiestl, R. H. (2001). "Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in Saccharomyces cerevisiae." Mol Cell Biol 21:8483-8489.11713283
  • Pahlman, I. L., Larsson, C., Averet, N., Bunoust, O., Boubekeur, S., Gustafsson, L., Rigoulet, M. (2002). "Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae." J Biol Chem 277:27991-27995.12032156
  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278