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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
membrane part
intrinsic to membrane
integral to membrane
cell part
Function
cofactor binding
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
NADP or NADPH binding
binding
coenzyme binding
nucleotide binding
oxidoreductase activity
hydroxymethylglutaryl-CoA reductase (NADPH) activity
catalytic activity
Process
coenzyme A metabolic process
cellular metabolic process
primary metabolic process
lipid metabolic process
cellular lipid metabolic process
oxidation reduction
isoprenoid metabolic process
metabolic process
cofactor metabolic process
isoprenoid biosynthetic 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