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NADH-cytochrome b5 reductase 1 (P38626)

Identification
NameNADH-cytochrome b5 reductase 1
Synonyms
  • Microsomal cytochrome b reductase
  • P35
Gene NameCBR1
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionElectron donor reductase for cytochrome b5. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. Plays a role in bud morphology
Cellular LocationEndoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion outer membrane; Single-pass membrane protein (Potential)
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
catalytic activity
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>YIL043C CBR1 SGDID:S000001305, Chr IX from 274926-274072, reverse complement, Verified ORF, "Microsomal cytochrome b reductase, not essential for viability; also detected in mitochondria; mutation in conserved NADH binding domain of the human ortholog res ATGGCTATTGATGCTCAAAAGCTTGTGGTGGTCATCGTGATCGTGGTCGTGCCTTTGCTC TTCAAGTTCATTATCGGACCGAAGACCAAGCCTGTGCTGGATCCCAAAAGGAATGACTTC CAATCATTTCCGCTGGTTGAAAAAACCATCTTAACGCATAATACTTCGATGTACAAGTTC GGGCTACCTCATGCTGACGACGTACTCGGTTTACCAATTGGTCAGCATATCGTAATTAAG GCCAATATCAATGGTAAGGATATTACCAGATCGTATACGCCCACATCGTTGGATGGAGAT ACAAAGGGAAACTTTGAATTACTAGTGAAGTCTTACCCCACAGGTAACGTTTCTAAGATG ATTGGAGAGTTGAAGATAGGTGACTCGATCCAGATCAAGGGCCCTCGTGGGAACTATCAT TATGAGAGAAACTGCCGTTCCCATCTAGGGATGATTGCTGGTGGTACTGGTATTGCGCCC ATGTATCAGATCATGAAAGCTATTGCCATGGACCCTCACGACACTACCAAGGTCTCTCTA GTCTTTGGGAACGTCCATGAGGAGGATATTCTGTTGAAGAAGGAACTGGAAGCGTTGGTG GCCATGAAGCCTTCCCAATTTAAGATAGTTTACTACTTAGACTCTCCTGACCGTGAAGAC TGGACTGGTGGTGTAGGATACATTACCAAGGATGTCATCAAGGAACACTTGCCCGCTGCT ACAATGGACAACGTTCAAATTTTGATCTGTGGTCCTCCAGCCATGGTTGCCTCAGTTAGA AGAAGTACCGTGGACTTGGGGTTCAGACGTTCCAAACCGCTTTCCAAGATGGAAGACCAG GTGTTTGTGTTTTAA
Protein Properties
Pfam Domain Function
Protein Residues284
Protein Molecular Weight31493.59961
Protein Theoretical pI9.19
Signalling Regions
  • None
Transmembrane Regions
  • 7-27
Protein Sequence>NADH-cytochrome b5 reductase 1 MAIDAQKLVVVIVIVVVPLLFKFIIGPKTKPVLDPKRNDFQSFPLVEKTILTHNTSMYKF GLPHADDVLGLPIGQHIVIKANINGKDITRSYTPTSLDGDTKGNFELLVKSYPTGNVSKM IGELKIGDSIQIKGPRGNYHYERNCRSHLGMIAGGTGIAPMYQIMKAIAMDPHDTTKVSL VFGNVHEEDILLKKELEALVAMKPSQFKIVYYLDSPDREDWTGGVGYITKDVIKEHLPAA TMDNVQILICGPPAMVASVRRSTVDLGFRRSKPLSKMEDQVFVF
References
External Links
ResourceLink
Saccharomyces Genome Database CBR1
Uniprot IDP38626
Uniprot NameNCB5R_YEAST
General Reference
  • Csukai, M., Murray, M., Orr, E. (1994). "Isolation and complete sequence of CBR, a gene encoding a putative cytochrome b reductase in Saccharomyces cerevisiae." Eur J Biochem 219:441-448.8307010
  • Churcher, C., Bowman, S., Badcock, K., Bankier, A., Brown, D., Chillingworth, T., Connor, R., Devlin, K., Gentles, S., Hamlin, N., Harris, D., Horsnell, T., Hunt, S., Jagels, K., Jones, M., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Rowley, N., Skelton, J., Smith, V., Barrell, B., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Nature 387:84-87.9169870
  • Kubota, S., Yoshida, Y., Kumaoka, H. (1977). "Studies on the microsomal electron-transport system of anaerobically grown yeast. IV. Purification and characterization of NADH-cytochrome b5 reductase." J Biochem 81:187-195.14930
  • Bertrand, J. C., Mattei, G., Parra, C., Giordani, R., Gilewicz, M. (1984). "Influence of oxygen on the microsomal electron transport system in Saccharomyces cerevisiae." Biochimie 66:583-588.6442167
  • Lamb, D. C., Kelly, D. E., Manning, N. J., Kaderbhai, M. A., Kelly, S. L. (1999). "Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction." FEBS Lett 462:283-288.10622712
  • Kellis, M., Patterson, N., Endrizzi, M., Birren, B., Lander, E. S. (2003). "Sequencing and comparison of yeast species to identify genes and regulatory elements." Nature 423:241-254.12748633
  • 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
  • Zhang, Z., Dietrich, F. S. (2005). "Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE." Nucleic Acids Res 33:2838-2851.15905473
  • 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
  • Tiedje, C., Holland, D. G., Just, U., Hofken, T. (2007). "Proteins involved in sterol synthesis interact with Ste20 and regulate cell polarity." J Cell Sci 120:3613-3624.17895367