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Identification
NameNADH-cytochrome b5 reductase 2
Synonyms
  • Mitochondrial cytochrome b reductase
  • p34/p32
  • NADH-cytochrome b5 reductase p34 form
  • NADH-cytochrome b5 reductase p32 form
Gene NameMCR1
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionThe outer membrane form may mediate the reduction of outer membrane cytochrome b5, and the soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals
Cellular LocationNADH-cytochrome b5 reductase p34 form:Mitochondrion outer membrane; Single-pass membrane protein
SMPDB Pathways
Amino sugar and nucleotide sugar metabolismPW002413 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Amino sugar and nucleotide sugar metabolismec00520 Map00520
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00110NADShow
YMDB00143NADHShow
YMDB00412NAD(+)Show
YMDB00605ergosta-5,7,24(28)-trien-3beta-olShow
YMDB00606ergosta-5,7,22,24(28)-tetraen-3beta-olShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB00900oxygenShow
GO Classification
Component
Not Available
Function
oxidoreductase activity
catalytic activity
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome Locationchromosome 11
LocusYKL150W
Gene Sequence>909 bp ATGTTTTCCAGATTATCCAGATCTCACTCAAAAGCATTACCGATTGCTCTAGGTACAGTT GCTATAGCAGCTGCTACCGCATTCTATTTTGCAAACCGTAACCAACATTCCTTTGTCTTC AATGAATCCAATAAAGTATTCAAGGGTGATGACAAATGGATCGACTTGCCAATATCTAAA ATAGAGGAGGAATCCCACGACACCAGAAGGTTTACTTTTAAGCTGCCTACTGAAGACTCA GAAATGGGGTTGGTCCTAGCATCTGCTCTGTTTGCTAAATTTGTCACACCAAAGGGATCC AATGTGGTGAGACCATACACTCCTGTGAGTGATCTTTCCCAGAAGGGTCACTTCCAGCTG GTCGTCAAGCATTATGAAGGTGGTAAAATGACCTCACATTTATTTGGTCTTAAACCAAAT GACACCGTTTCTTTCAAGGGTCCTATTATGAAATGGAAGTGGCAACCTAATCAGTTCAAG TCAATCACCTTGTTAGGTGCCGGTACCGGTATCAACCCTCTGTACCAATTAGCTCATCAT ATAGTTGAAAACCCAAACGACAAGACCAAAGTTAACTTGCTATATGGGAACAAGACTCCT CAGGACATTTTACTAAGGAAGGAACTGGATGCGTTGAAGGAAAAGTATCCTGACAAGTTC AATGTTACTTACTTTGTTGACGACAAGCAAGATGACCAAGACTTTGATGGTGAAATTAGT TTCATCTCCAAAGATTTTATTCAGGAGCATGTTCCAGGTCCAAAGGAAAGCACACATTTG TTTGTCTGCGGTCCCCCACCATTTATGAACGCTTACTCAGGTGAGAAGAAGTCACCTAAG GACCAAGGTGAATTGATCGGTATCTTGAACAATTTGGGCTACTCCAAGGACCAAGTTTTC AAATTTTAA
Protein Properties
Pfam Domain Function
Protein Residues302
Protein Molecular Weight34137.69922
Protein Theoretical pI9.11
Signalling Regions
  • None
Transmembrane Regions
  • 12-32
Protein Sequence>NADH-cytochrome b5 reductase 2 MFSRLSRSHSKALPIALGTVAIAAATAFYFANRNQHSFVFNESNKVFKGDDKWIDLPISK IEEESHDTRRFTFKLPTEDSEMGLVLASALFAKFVTPKGSNVVRPYTPVSDLSQKGHFQL VVKHYEGGKMTSHLFGLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHH IVENPNDKTKVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGEIS FISKDFIQEHVPGPKESTHLFVCGPPPFMNAYSGEKKSPKDQGELIGILNNLGYSKDQVF KF
References
External Links
ResourceLink
Saccharomyces Genome Database MCR1
Uniprot IDP36060
Uniprot NameMCR1_YEAST
GenBank Gene IDX81474
Genebank Protein ID1490392
General Reference
  • Hahne, K., Haucke, V., Ramage, L., Schatz, G. (1994). "Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments." Cell 79:829-839.8001120
  • Vandenbol, M., Bolle, P. A., Dion, C., Portetelle, D., Hilger, F. (1994). "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci of chromosome XI of Saccharomyces cerevisiae." Yeast 10 Suppl A:S35-S40.8091859
  • Dujon, B., Alexandraki, D., Andre, B., Ansorge, W., Baladron, V., Ballesta, J. P., Banrevi, A., Bolle, P. A., Bolotin-Fukuhara, M., Bossier, P., et, a. l. .. (1994). "Complete DNA sequence of yeast chromosome XI." Nature 369:371-378.8196765
  • Juneau, K., Palm, C., Miranda, M., Davis, R. W. (2007). "High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing." Proc Natl Acad Sci U S A 104:1522-1527.17244705
  • Burri, L., Vascotto, K., Gentle, I. E., Chan, N. C., Beilharz, T., Stapleton, D. I., Ramage, L., Lithgow, T. (2006). "Integral membrane proteins in the mitochondrial outer membrane of Saccharomyces cerevisiae." FEBS J 273:1507-1515.16689936
  • Martin, H., Eckerskorn, C., Gartner, F., Rassow, J., Lottspeich, F., Pfanner, N. (1998). "The yeast mitochondrial intermembrane space: purification and analysis of two distinct fractions." Anal Biochem 265:123-128.9866716
  • Haucke, V., Ocana, C. S., Honlinger, A., Tokatlidis, K., Pfanner, N., Schatz, G. (1997). "Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria." Mol Cell Biol 17:4024-4032.9199337
  • Lee, J. S., Huh, W. K., Lee, B. H., Baek, Y. U., Hwang, C. S., Kim, S. T., Kim, Y. R., Kang, S. O. (2001). "Mitochondrial NADH-cytochrome b(5) reductase plays a crucial role in the reduction of D-erythroascorbyl free radical in Saccharomyces cerevisiae." Biochim Biophys Acta 1527:31-38.11420140
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • 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
  • Krantz, M., Nordlander, B., Valadi, H., Johansson, M., Gustafsson, L., Hohmann, S. (2004). "Anaerobicity prepares Saccharomyces cerevisiae cells for faster adaptation to osmotic shock." Eukaryot Cell 3:1381-1390.15590813
  • Zahedi, R. P., Sickmann, A., Boehm, A. M., Winkler, C., Zufall, N., Schonfisch, B., Guiard, B., Pfanner, N., Meisinger, C. (2006). "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins." Mol Biol Cell 17:1436-1450.16407407
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950