External NADH-ubiquinone oxidoreductase 1, mitochondrial (P40215)

Identification
NameExternal NADH-ubiquinone oxidoreductase 1, mitochondrial
Synonyms
  • External NADH dehydrogenase 1
Gene NameNDE1
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 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
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 + hydron → NAD + 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
metabolic process
oxidation reduction
Gene Properties
Chromosome Locationchromosome 13
LocusYMR145C
Gene Sequence>1683 bp ATGATTAGACAATCATTAATGAAAACAGTGTGGGCTAACTCCTCCAGGTTTAGCCTACAG AGCAAGTCGGGGCTTGTGAAATATGCCAAAAATAGATCGTTCCATGCAGCAAGAAATTTG CTAGAGGACAAGAAAGTCATTTTGCAAAAAGTGGCGCCCACTACTGGCGTTGTTGCGAAG CAGTCCTTTTTCAAGAGAACTGGGAAATTTACTTTGAAGGCTTTATTGTATTCTGCCCTC GCGGGTACGGCTTACGTTTCATACTCACTTTACCGAGAAGCTAACCCTTCTACCCAAGTT CCTCAATCGGACACTTTTCCAAACGGTTCAAAGAGGAAGACTTTGGTAATTCTGGGCTCC GGTTGGGGTTCTGTGTCGCTTTTGAAAAATTTGGACACCACGTTGTATAATGTTGTTGTT GTTTCTCCAAGAAATTATTTTCTTTTTACTCCGCTATTGCCATCTACCCCAGTTGGTACC ATCGAATTGAAATCTATTGTTGAACCTGTCAGGACTATTGCTAGAAGATCGCACGGTGAA GTCCATTACTATGAAGCTGAAGCGTACGACGTTGATCCTGAAAACAAAACAATTAAGGTC AAATCTTCCGCTAAGAATAACGACTACGACTTGGACTTGAAATACGACTATCTGGTTGTC GGTGTGGGTGCTCAACCAAACACTTTTGGTACTCCGGGAGTTTATGAATATTCTTCTTTC TTGAAGGAAATATCCGACGCTCAAGAGATCAGATTAAAAATTATGTCCAGTATTGAGAAA GCTGCCTCCCTATCTCCAAAAGATCCTGAGAGAGCAAGATTGTTGAGCTTTGTTGTCGTT GGTGGTGGTCCCACCGGTGTCGAATTTGCCGCTGAATTGAGAGATTATGTTGACCAGGAC TTGAGAAAATGGATGCCCGAATTGAGTAAAGAAATTAAAGTCACTTTGGTGGAGGCTTTG CCAAACATTTTGAACATGTTTGACAAGTATCTCGTTGACTATGCTCAAGATTTATTCAAA GAGGAAAAAATCGATTTAAGATTGAAAACAATGGTTAAGAAAGTTGACGCTACCACTATA ACTGCCAAAACTGGCGATGGTGACATTGAAAATATACCGTATGGTGTATTAGTTTGGGCT ACAGGTAATGCGCCAAGAGAAGTGTCTAAGAACCTAATGACTAAATTAGAGGAACAGGAC TCAAGACGTGGTTTGTTGATAGATAACAAACTTCAACTTTTGGGTGCTAAGGGATCTATT TTTGCTATCGGCGATTGTACCTTCCACCCTGGCTTGTTCCCTACCGCTCAAGTTGCCCAC CAAGAAGGTGAATACTTGGCTCAGTATTTCAAGAAAGCTTATAAAATCGATCAATTGAAC TGGAAAATGACCCATGCTAAAGACGATTCAGAAGTCGCTAGATTAAAGAACCAAATAGTC AAAACGCAATCGCAAATTGAAGACTTCAAGTACAACCATAAGGGTGCTCTGGCTTATATT GGTTCAGATAAAGCCATTGCTGATCTTGCCGTTGGTGAAGCCAAATATAGGTTAGCCGGC TCATTCACCTTCCTATTCTGGAAATCTGCTTATTTGGCAATGTGTCTATCCTTTAGAAAC AGAGTTCTTGTCGCTATGGATTGGGCTAAAGTTTATTTCTTGGGTAGAGATTCATCTATC TAG
Protein Properties
Pfam Domain Function
Protein Residues560
Protein Molecular Weight62773.60156
Protein Theoretical pI9.73
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>External NADH-ubiquinone oxidoreductase 1, mitochondrial MIRQSLMKTVWANSSRFSLQSKSGLVKYAKNRSFHAARNLLEDKKVILQKVAPTTGVVAK QSFFKRTGKFTLKALLYSALAGTAYVSYSLYREANPSTQVPQSDTFPNGSKRKTLVILGS GWGSVSLLKNLDTTLYNVVVVSPRNYFLFTPLLPSTPVGTIELKSIVEPVRTIARRSHGE VHYYEAEAYDVDPENKTIKVKSSAKNNDYDLDLKYDYLVVGVGAQPNTFGTPGVYEYSSF LKEISDAQEIRLKIMSSIEKAASLSPKDPERARLLSFVVVGGGPTGVEFAAELRDYVDQD LRKWMPELSKEIKVTLVEALPNILNMFDKYLVDYAQDLFKEEKIDLRLKTMVKKVDATTI TAKTGDGDIENIPYGVLVWATGNAPREVSKNLMTKLEEQDSRRGLLIDNKLQLLGAKGSI FAIGDCTFHPGLFPTAQVAHQEGEYLAQYFKKAYKIDQLNWKMTHAKDDSEVARLKNQIV KTQSQIEDFKYNHKGALAYIGSDKAIADLAVGEAKYRLAGSFTFLFWKSAYLAMCLSFRN RVLVAMDWAKVYFLGRDSSI
References
External Links
ResourceLink
Saccharomyces Genome Database NDE1
Uniprot IDP40215
Uniprot NameNDH1_YEAST
GenBank Gene IDAY692785
Genebank Protein ID51013021
General Reference
  • Bowman, S., Churcher, C., 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., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., 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., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • 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
  • Small, W. C., McAlister-Henn, L. (1998). "Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae." J Bacteriol 180:4051-4055.9696750
  • 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
  • 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
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • 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