3-keto-steroid reductase (Q12452)

Identification
Name3-keto-steroid reductase
SynonymsNot Available
Gene NameERG27
Enzyme Class
Biological Properties
General FunctionInvolved in binding
Specific FunctionResponsible for the reduction of the keto group on the C-3 of sterols. Also facilitates the association of ERG7 with lipid particles preventing its digestion in the endoplasmic reticulum and the lipid particles
Cellular LocationEndoplasmic reticulum membrane; Peripheral membrane protein. Lipid droplet
SMPDB Pathways
Cholesterol biosynthesis and metabolism CE(10:0)PW002545 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(12:0)PW002548 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(14:0)PW002544 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(16:0)PW002550 ThumbThumb?image type=greyscaleThumb?image type=simple
Cholesterol biosynthesis and metabolism CE(18:0)PW002551 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Steroid biosynthesisec00100 Map00100
SMPDB Reactions
3-Keto-4-methylzymosterol + NADPH → 4alpha-methylzymosterol + NADP
3-Keto-4-methylzymosterol + NADPH + hydron → NADP + 4alpha-methylzymosterol
zymosterol intermediate 2 + NADPH + hydron → zymosterol + NADP
KEGG Reactions
3-dehydro-4-methylzymosterol + NADPH + hydron → NADP + 4alpha-methylzymosterol
zymosterol intermediate 2 + NADPH + hydron → NADP + zymosterol
Metabolites
YMDB IDNameView
YMDB000364-alpha-Methyl-5-alpha-cholest-7-en-3-beta-ol Show
YMDB001864-alpha-Methyl-5-alpha-cholest-7-en-3-oneShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00548zymosterolShow
YMDB00608zymosterol intermediate 2Show
YMDB006093-dehydro-4-methylzymosterolShow
YMDB006114alpha-methylzymosterolShow
YMDB00862hydronShow
YMDB161913-Keto-4-methylzymosterolShow
GO Classification
Component
Not Available
Function
catalytic activity
binding
oxidoreductase activity
Process
metabolic process
Gene Properties
Chromosome Locationchromosome 12
LocusYLR100W
Gene Sequence>1044 bp ATGAACAGGAAAGTAGCTATCGTAACGGGTACTAATAGTAATCTTGGTCTGAACATTGTG TTCCGTCTGATTGAAACTGAGGACACCAATGTCAGATTGACCATTGTGGTGACTTCTAGA ACGCTTCCTCGAGTGCAGGAGGTGATTAACCAGATTAAAGATTTTTACAACAAATCAGGC CGTGTAGAGGATTTGGAAATAGACTTTGATTATCTGTTGGTGGACTTCACCAACATGGTG AGTGTCTTGAACGCATATTACGACATCAACAAAAAGTACAGGGCGATAAACTACCTTTTC GTGAATGCTGCGCAAGGTATCTTTGACGGTATAGATTGGATCGGAGCGGTCAAGGAGGTT TTCACCAATCCATTGGAGGCAGTGACAAATCCGACATACAAGATACAACTGGTGGGCGTC AAGTCTAAAGATGACATGGGGCTTATTTTCCAGGCCAATGTGTTTGGTCCGTACTACTTT ATCAGTAAAATTCTGCCTCAATTGACCAGGGGAAAGGCTTATATTGTTTGGATTTCGAGT ATTATGTCCGATCCTAAGTATCTTTCGTTGAACGATATTGAACTACTAAAGACAAATGCC TCTTATGAGGGCTCCAAGCGTTTAGTTGATTTACTGCATTTGGCCACCTACAAAGACTTG AAAAAGCTGGGCATAAATCAGTATGTAGTTCAACCGGGCATATTTACAAGCCATTCCTTC TCCGAATATTTGAATTTTTTCACCTATTTCGGCATGCTATGCTTGTTCTATTTGGCCAGG CTGTTGGGGTCTCCATGGCACAATATTGATGGTTATAAAGCTGCCAATGCCCCAGTATAC GTAACTAGATTGGCCAATCCAAACTTTGAGAAACAAGACGTAAAATACGGTTCTGCTACC TCTAGGGATGGTATGCCATATATCAAGACGCAGGAAATAGACCCTACTGGAATGTCTGAT GTCTTCGCTTATATACAGAAGAAGAAACTGGAATGGGACGAGAAACTGAAAGATCAAATT GTTGAAACTAGAACCCCCATTTAA
Protein Properties
Pfam Domain FunctionNot Available
Protein Residues347
Protein Molecular Weight39724.39844
Protein Theoretical pI8.64
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>3-keto-steroid reductase MNRKVAIVTGTNSNLGLNIVFRLIETEDTNVRLTIVVTSRTLPRVQEVINQIKDFYNKSG RVEDLEIDFDYLLVDFTNMVSVLNAYYDINKKYRAINYLFVNAAQGIFDGIDWIGAVKEV FTNPLEAVTNPTYKIQLVGVKSKDDMGLIFQANVFGPYYFISKILPQLTRGKAYIVWISS IMSDPKYLSLNDIELLKTNASYEGSKRLVDLLHLATYKDLKKLGINQYVVQPGIFTSHSF SEYLNFFTYFGMLCLFYLARLLGSPWHNIDGYKAANAPVYVTRLANPNFEKQDVKYGSAT SRDGMPYIKTQEIDPTGMSDVFAYIQKKKLEWDEKLKDQIVETRTPI
References
External Links
ResourceLink
Saccharomyces Genome Database ERG27
Uniprot IDQ12452
Uniprot NameERG27_YEAST
GenBank Gene IDU53876
Genebank Protein ID1256850
General Reference
  • Johnston, M., Hillier, L., Riles, L., Albermann, K., Andre, B., Ansorge, W., Benes, V., Bruckner, M., Delius, H., Dubois, E., Dusterhoft, A., Entian, K. D., Floeth, M., Goffeau, A., Hebling, U., Heumann, K., Heuss-Neitzel, D., Hilbert, H., Hilger, F., Kleine, K., Kotter, P., Louis, E. J., Messenguy, F., Mewes, H. W., Hoheisel, J. D., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Nature 387:87-90.9169871
  • Gachotte, D., Sen, S. E., Eckstein, J., Barbuch, R., Krieger, M., Ray, B. D., Bard, M. (1999). "Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation." Proc Natl Acad Sci U S A 96:12655-12660.10535978
  • Mo, C., Valachovic, M., Randall, S. K., Nickels, J. T., Bard, M. (2002). "Protein-protein interactions among C-4 demethylation enzymes involved in yeast sterol biosynthesis." Proc Natl Acad Sci U S A 99:9739-9744.12119386
  • Mo, C., Milla, P., Athenstaedt, K., Ott, R., Balliano, G., Daum, G., Bard, M. (2003). "In yeast sterol biosynthesis the 3-keto reductase protein (Erg27p) is required for oxidosqualene cyclase (Erg7p) activity." Biochim Biophys Acta 1633:68-74.12842197
  • Mo, C., Bard, M. (2005). "Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex." J Lipid Res 46:1991-1998.15995173
  • Natter, K., Leitner, P., Faschinger, A., Wolinski, H., McCraith, S., Fields, S., Kohlwein, S. D. (2005). "The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy." Mol Cell Proteomics 4:662-672.15716577
  • 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
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356