Lanosterol 14-alpha demethylase (P10614)

Identification
NameLanosterol 14-alpha demethylase
Synonyms
  • CYPLI
  • Cytochrome P450 51
  • Cytochrome P450-14DM
  • Cytochrome P450-LIA1
  • Sterol 14-alpha demethylase
Gene NameERG11
Enzyme Class
Biological Properties
General FunctionInvolved in iron ion binding
Specific FunctionCatalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol
Cellular LocationMembrane; Single-pass membrane protein
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
Lanosterin + oxygen + NADPH → 4,4-Dimethylcholesta-8,14,24-trienol + Formic acid + NADP + water
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00015Delta 8,14 -SterolShow
YMDB00110NADShow
YMDB00143NADHShow
YMDB00180ObtusifoliolShow
YMDB00262LanosterinShow
YMDB002684,4-Dimethylcholesta-8,14,24-trienolShow
YMDB00385Formic acidShow
YMDB00412NAD(+)Show
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00547lanosterolShow
YMDB006034,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-olShow
YMDB0084224,25-dihydrolanosterolShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB00900oxygenShow
GO Classification
Component
Not Available
Function
catalytic activity
binding
ion binding
cation binding
metal ion binding
transition metal ion binding
iron ion binding
oxidoreductase activity
heme binding
electron carrier activity
monooxygenase activity
Process
Not Available
Gene Properties
Chromosome Locationchromosome 8
LocusYHR007C
Gene Sequence>1593 bp ATGTCTGCTACCAAGTCAATCGTTGGAGAGGCATTGGAATACGTAAACATTGGTTTAAGT CATTTCTTGGCTTTACCATTGGCCCAAAGAATCTCTTTGATCATAATAATTCCTTTCATT TACAATATTGTATGGCAATTACTATATTCTTTGAGAAAGGACCGTCCACCTCTAGTGTTT TACTGGATTCCATGGGTCGGTAGTGCTGTTGTGTACGGTATGAAGCCATACGAGTTTTTC GAAGAATGTCAAAAGAAATACGGTGATATTTTTTCATTCGTTTTGTTAGGAAGAGTCATG ACTGTGTATTTAGGACCAAAGGGTCACGAATTTGTCTTCAACGCTAAGTTGGCAGATGTT TCAGCAGAAGCTGCTTACGCTCATTTGACTACTCCAGTTTTCGGTAAAGGTGTTATTTAC GATTGTCCAAATTCTAGATTGATGGAGCAAAAGAAGTTTGTTAAGGGTGCTCTAACCAAA GAAGCCTTCAAGAGCTACGTTCCATTGATTGCTGAAGAAGTGTACAAGTACTTCAGAGAC TCCAAAAACTTCCGTTTGAATGAAAGAACTACTGGTACTATTGACGTGATGGTTACTCAA CCTGAAATGACTATTTTCACCGCTTCAAGATCATTATTGGGTAAGGAAATGAGAGCAAAA TTGGATACCGATTTTGCTTACTTGTACAGTGATTTGGATAAGGGTTTCACTCCAATCAAC TTCGTCTTCCCTAACTTACCATTGGAACACTATAGAAAGAGAGATCACGCTCAAAAGGCT ATCTCCGGTACTTACATGTCTTTGATTAAGGAAAGAAGAAAGAACAACGACATTCAAGAC AGAGATTTGATCGATTCCTTGATGAAGAACTCTACCTACAAGGATGGTGTGAAGATGACT GATCAAGAAATCGCTAACTTGTTAATTGGTGTCTTAATGGGTGGTCAACATACTTCTGCT GCCACTTCTGCTTGGATTTTGTTGCACTTGGCTGAAAGACCAGATGTCCAACAAGAATTG TACGAAGAACAAATGCGTGTTTTGGATGGTGGTAAGAAGGAATTGACCTACGATTTATTA CAAGAAATGCCATTGTTGAACCAAACTATTAAGGAAACTCTAAGAATGCACCATCCATTG CACTCTTTGTTCCGTAAGGTTATGAAAGATATGCACGTTCCAAACACTTCTTATGTCATC CCAGCAGGTTATCACGTTTTGGTTTCTCCAGGTTACACTCATTTAAGAGACGAATACTTC CCTAATGCTCACCAATTCAACATTCACCGTTGGAACAAAGATTCTGCCTCCTCTTATTCC GTCGGTGAAGAAGTCGATTACGGTTTCGGTGCCATTTCTAAGGGTGTCAGCTCTCCATAC TTACCTTTCGGTGGTGGTAGACACAGATGTATCGGTGAACACTTTGCTTACTGTCAGCTA GGTGTTCTAATGTCCATTTTTATCAGAACATTAAAATGGCATTACCCAGAGGGTAAGACC GTTCCACCTCCTGACTTTACATCTATGGTTACTCTTCCAACCGGTCCAGCCAAGATCATC TGGGAAAAGAGAAATCCAGAACAAAAGATCTAA
Protein Properties
Pfam Domain Function
Protein Residues530
Protein Molecular Weight60719.80078
Protein Theoretical pI8.95
Signalling Regions
  • None
Transmembrane Regions
  • 21-41
Protein Sequence>Lanosterol 14-alpha demethylase MSATKSIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPPLVF YWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPKGHEFVFNAKLADV SAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGALTKEAFKSYVPLIAEEVYKYFRD SKNFRLNERTTGTIDVMVTQPEMTIFTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPIN FVFPNLPLEHYRKRDHAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMT DQEIANLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTYDLL QEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVLVSPGYTHLRDEYF PNAHQFNIHRWNKDSASSYSVGEEVDYGFGAISKGVSSPYLPFGGGRHRCIGEHFAYCQL GVLMSIFIRTLKWHYPEGKTVPPPDFTSMVTLPTGPAKIIWEKRNPEQKI
References
External Links
ResourceLink
Saccharomyces Genome Database ERG11
Uniprot IDP10614
Uniprot NameCP51_YEAST
GenBank Gene IDM18109
Genebank Protein ID170946
General Reference
  • Kalb, V. F., Woods, C. W., Turi, T. G., Dey, C. R., Sutter, T. R., Loper, J. C. (1987). "Primary structure of the P450 lanosterol demethylase gene from Saccharomyces cerevisiae." DNA 6:529-537.3322742
  • Ishida, N., Aoyama, Y., Hatanaka, R., Oyama, Y., Imajo, S., Ishiguro, M., Oshima, T., Nakazato, H., Noguchi, T., Maitra, U. S., et, a. l. .. (1988). "A single amino acid substitution converts cytochrome P450(14DM) to an inactive form, cytochrome P450SG1: complete primary structures deduced from cloned DNAS." Biochem Biophys Res Commun 155:317-323.3046615
  • Johnston, M., Andrews, S., Brinkman, R., Cooper, J., Ding, H., Dover, J., Du, Z., Favello, A., Fulton, L., Gattung, S., et, a. l. .. (1994). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Science 265:2077-2082.8091229
  • Kalb, V. F., Loper, J. C., Dey, C. R., Woods, C. W., Sutter, T. R. (1986). "Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae." Gene 45:237-245.3542713
  • 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
  • Mo, C., Bard, M. (2005). "Erg28p is a key protein in the yeast sterol biosynthetic enzyme complex." J Lipid Res 46:1991-1998.15995173
  • Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258
  • 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
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956