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Identification
Name3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
Synonyms
  • HMG-CoA reductase 1
Gene NameHMG1
Enzyme Class
Biological Properties
General FunctionInvolved in hydroxymethylglutaryl-CoA reductase (NADPH) activity
Specific FunctionThis transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of the sterol biosynthesis
Cellular LocationEndoplasmic reticulum membrane; Multi-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
Terpenoid backbone biosynthesisec00900 Map00900
SMPDB Reactions
3-Hydroxy-3-methylglutaryl-CoA + NADPH(R)-Mevalonic acid + NADP + Coenzyme A
KEGG Reactions
NADP + (R)-Mevalonic acid + Coenzyme A3-Hydroxy-3-methylglutaryl-CoA + hydron + NADPH
Metabolites
YMDB IDNameView
YMDB00045Coenzyme AShow
YMDB0031022b-HydroxycholesterolShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00707(R)-Mevalonic acidShow
YMDB007083-Hydroxy-3-methylglutaryl-CoAShow
YMDB00862hydronShow
YMDB01039(R)-MevalonateShow
GO Classification
Component
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
catalytic activity
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
NADP or NADPH binding
coenzyme binding
hydroxymethylglutaryl-CoA reductase (NADPH) activity
binding
nucleotide binding
oxidoreductase activity
cofactor binding
oxidoreductase activity, acting on CH-OH group of donors
Process
metabolic process
lipid metabolic process
cellular lipid metabolic process
cellular metabolic process
isoprenoid metabolic process
isoprenoid biosynthetic process
primary metabolic process
coenzyme A metabolic process
oxidation reduction
cofactor metabolic process
coenzyme metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYML075C
Gene Sequence>3165 bp ATGCCGCCGCTATTCAAGGGACTGAAACAGATGGCAAAGCCAATTGCCTATGTTTCAAGA TTTTCGGCGAAACGACCAATTCATATAATACTTTTTTCTCTAATCATATCCGCATTCGCT TATCTATCCGTCATTCAGTATTACTTCAATGGTTGGCAACTAGATTCAAATAGTGTTTTT GAAACTGCTCCAAATAAAGACTCCAACACTCTATTTCAAGAATGTTCCCATTACTACAGA GATTCCTCTCTAGATGGTTGGGTATCAATCACCGCGCATGAAGCTAGTGAGTTACCAGCC CCACACCATTACTATCTATTAAACCTGAACTTCAATAGTCCTAATGAAACTGACTCCATT CCAGAACTAGCTAACACGGTTTTTGAGAAAGATAATACAAAATATATTCTGCAAGAAGAT CTCAGTGTTTCCAAAGAAATTTCTTCTACTGATGGAACGAAATGGAGGTTAAGAAGTGAC AGAAAAAGTCTTTTCGACGTAAAGACGTTAGCATATTCTCTCTACGATGTATTTTCAGAA AATGTAACCCAAGCAGACCCGTTTGACGTCCTTATTATGGTTACTGCCTACCTAATGATG TTCTACACCATATTCGGCCTCTTCAATGACATGAGGAAGACCGGGTCAAATTTTTGGTTG AGCGCCTCTACAGTGGTCAATTCTGCATCATCACTTTTCTTAGCATTGTATGTCACCCAA TGTATTCTAGGCAAAGAAGTTTCCGCATTAACTCTTTTTGAAGGTTTGCCTTTCATTGTA GTTGTTGTTGGTTTCAAGCACAAAATCAAGATTGCCCAGTATGCCCTGGAGAAATTTGAA AGAGTCGGTTTATCTAAAAGGATTACTACCGATGAAATCGTTTTTGAATCCGTGAGCGAA GAGGGTGGTCGTTTGATTCAAGACCATTTGCTTTGTATTTTTGCCTTTATCGGATGCTCT ATGTATGCTCACCAATTGAAGACTTTGACAAACTTCTGCATATTATCAGCATTTATCCTA ATTTTTGAATTGATTTTAACTCCTACATTTTATTCTGCTATCTTAGCGCTTAGACTGGAA ATGAATGTTATCCACAGATCTACTATTATCAAGCAAACATTAGAAGAAGACGGTGTTGTT CCATCTACAGCAAGAATCATTTCTAAAGCAGAAAAGAAATCCGTATCTTCTTTCTTAAAT CTCAGTGTGGTTGTCATTATCATGAAACTCTCTGTCATACTGTTGTTTGTCTTCATCAAC TTTTATAACTTTGGTGCAAATTGGGTCAATGATGCCTTCAATTCATTGTACTTCGATAAG GAACGTGTTTCTCTACCAGATTTTATTACCTCGAATGCCTCTGAAAACTTTAAAGAGCAA GCTATTGTTAGTGTCACCCCATTATTATATTACAAACCCATTAAGTCCTACCAACGCATT GAGGATATGGTTCTTCTATTGCTTCGTAATGTCAGTGTTGCCATTCGTGATAGGTTCGTC AGTAAATTAGTTCTTTCCGCCTTAGTATGCAGTGCTGTCATCAATGTGTATTTATTGAAT GCTGCTAGAATTCATACCAGTTATACTGCAGACCAATTGGTGAAAACTGAAGTCACCAAG AAGTCTTTTACTGCTCCTGTACAAAAGGCTTCTACACCAGTTTTAACCAATAAAACAGTC ATTTCTGGATCGAAAGTCAAAAGTTTATCATCTGCGCAATCGAGCTCATCAGGACCTTCA TCATCTAGTGAGGAAGATGATTCCCGCGATATTGAAAGCTTGGATAAGAAAATACGTCCT TTAGAAGAATTAGAAGCATTATTAAGTAGTGGAAATACAAAACAATTGAAGAACAAAGAG GTCGCTGCCTTGGTTATTCACGGTAAGTTACCTTTGTACGCTTTGGAGAAAAAATTAGGT GATACTACGAGAGCGGTTGCGGTACGTAGGAAGGCTCTTTCAATTTTGGCAGAAGCTCCT GTATTAGCATCTGATCGTTTACCATATAAAAATTATGACTACGACCGCGTATTTGGCGCT TGTTGTGAAAATGTTATAGGTTACATGCCTTTGCCCGTTGGTGTTATAGGCCCCTTGGTT ATCGATGGTACATCTTATCATATACCAATGGCAACTACAGAGGGTTGTTTGGTAGCTTCT GCCATGCGTGGCTGTAAGGCAATCAATGCTGGCGGTGGTGCAACAACTGTTTTAACTAAG GATGGTATGACAAGAGGCCCAGTAGTCCGTTTCCCAACTTTGAAAAGATCTGGTGCCTGT AAGATATGGTTAGACTCAGAAGAGGGACAAAACGCAATTAAAAAAGCTTTTAACTCTACA TCAAGATTTGCACGTCTGCAACATATTCAAACTTGTCTAGCAGGAGATTTACTCTTCATG AGATTTAGAACAACTACTGGTGACGCAATGGGTATGAATATGATTTCTAAAGGTGTCGAA TACTCATTAAAGCAAATGGTAGAAGAGTATGGCTGGGAAGATATGGAGGTTGTCTCCGTT TCTGGTAACTACTGTACCGACAAAAAACCAGCTGCCATCAACTGGATCGAAGGTCGTGGT AAGAGTGTCGTCGCAGAAGCTACTATTCCTGGTGATGTTGTCAGAAAAGTGTTAAAAAGT GATGTTTCCGCATTGGTTGAGTTGAACATTGCTAAGAATTTGGTTGGATCTGCAATGGCT GGGTCTGTTGGTGGATTTAACGCACATGCAGCTAATTTAGTGACAGCTGTTTTCTTGGCA TTAGGACAAGATCCTGCACAAAATGTTGAAAGTTCCAACTGTATAACATTGATGAAAGAA GTGGACGGTGATTTGAGAATTTCCGTATCCATGCCATCCATCGAAGTAGGTACCATCGGT GGTGGTACTGTTCTAGAACCACAAGGTGCCATGTTGGACTTATTAGGTGTAAGAGGCCCG CATGCTACCGCTCCTGGTACCAACGCACGTCAATTAGCAAGAATAGTTGCCTGTGCCGTC TTGGCAGGTGAATTATCCTTATGTGCTGCCCTAGCAGCCGGCCATTTGGTTCAAAGTCAT ATGACCCACAACAGGAAACCTGCTGAACCAACAAAACCTAACAATTTGGACGCCACTGAT ATAAATCGTTTGAAAGATGGGTCCGTCACCTGCATTAAATCCTAA
Protein Properties
Pfam Domain Function
Protein Residues1054
Protein Molecular Weight115624.0
Protein Theoretical pI8.09
Signalling Regions
  • None
Transmembrane Regions
  • 27-53
  • 187-211
  • 242-266
  • 300-324
  • 332-357
  • 398-422
  • 499-524
Protein Sequence>3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVF ETAPNKDSNTLFQECSHYYRDSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSI PELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSDRKSLFDVKTLAYSLYDVFSE NVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQ CILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSE EGGRLIQDHLLCIFAFIGCSMYAHQLKTLTNFCILSAFILIFELILTPTFYSAILALRLE MNVIHRSTIIKQTLEEDGVVPSTARIISKAEKKSVSSFLNLSVVVIIMKLSVILLFVFIN FYNFGANWVNDAFNSLYFDKERVSLPDFITSNASENFKEQAIVSVTPLLYYKPIKSYQRI EDMVLLLLRNVSVAIRDRFVSKLVLSALVCSAVINVYLLNAARIHTSYTADQLVKTEVTK KSFTAPVQKASTPVLTNKTVISGSKVKSLSSAQSSSSGPSSSSEEDDSRDIESLDKKIRP LEELEALLSSGNTKQLKNKEVAALVIHGKLPLYALEKKLGDTTRAVAVRRKALSILAEAP VLASDRLPYKNYDYDRVFGACCENVIGYMPLPVGVIGPLVIDGTSYHIPMATTEGCLVAS AMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLKRSGACKIWLDSEEGQNAIKKAFNST SRFARLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSV SGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVRKVLKSDVSALVELNIAKNLVGSAMA GSVGGFNAHAANLVTAVFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIG GGTVLEPQGAMLDLLGVRGPHATAPGTNARQLARIVACAVLAGELSLCAALAAGHLVQSH MTHNRKPAEPTKPNNLDATDINRLKDGSVTCIKS
References
External Links
ResourceLink
Saccharomyces Genome Database HMG1
Uniprot IDP12683
Uniprot NameHMDH1_YEAST
GenBank Gene IDM22002
Genebank Protein ID171686
General Reference
  • Basson, M. E., Thorsness, M., Finer-Moore, J., Stroud, R. M., Rine, J. (1988). "Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol biosynthesis." Mol Cell Biol 8:3797-3808.3065625
  • 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
  • Basson, M. E., Thorsness, M., Rine, J. (1986). "Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase." Proc Natl Acad Sci U S A 83:5563-5567.3526336
  • 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
  • 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