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Identification
Name3-hydroxy-3-methylglutaryl-coenzyme A reductase 2
Synonyms
  • HMG-CoA reductase 2
Gene NameHMG2
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
cofactor binding
oxidoreductase activity, acting on CH-OH group of donors
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
Process
cofactor metabolic process
coenzyme metabolic 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
Gene Properties
Chromosome Locationchromosome 12
LocusYLR450W
Gene Sequence>3138 bp ATGTCACTTCCCTTAAAAACGATAGTACATTTGGTAAAGCCCTTTGCTTGCACTGCTAGG TTTAGTGCGAGATACCCAATCCACGTCATTGTTGTTGCTGTTTTATTGAGTGCCGCTGCT TATCTATCCGTGACACAATCTTACCTTAACGAATGGAAGCTGGACTCTAATCAGTATTCT ACATACTTAAGCATAAAGCCGGATGAGTTGTTTGAAAAATGCACACACTACTATAGGTCT CCTGTGTCTGATACATGGAAGTTACTCAGCTCTAAAGAAGCCGCCGATATTTATACCCCT TTTCATTATTATTTGTCTACCATAAGTTTTCAAAGTAAGGACAATTCAACGACTTTGCCT TCCCTTGATGACGTTATTTACAGTGTTGACCATACCAGGTACTTATTAAGTGAAGAGCCA AAGATACCAACTGAACTAGTGTCTGAAAACGGAACGAAATGGAGATTGAGAAACAACAGC AATTTTATTTTGGACCTGCATAATATTTACCGAAATATGGTGAAGCAATTTTCTAACAAA ACGAGCGAATTTGATCAGTTCGATTTGTTTATCATCCTAGCTGCTTACCTTACTCTTTTT TATACTCTCTGTTGCCTGTTTAATGACATGAGGAAAATCGGATCAAAGTTTTGGTTAAGC TTTTCTGCTCTTTCAAACTCTGCATGCGCATTATATTTATCGCTGTACACAACTCACAGT TTATTGAAGAAACCGGCTTCCTTATTAAGTTTGGTCATTGGACTACCATTTATCGTAGTA ATTATTGGCTTTAAGCATAAAGTTCGACTTGCGGCATTCTCGCTACAAAAATTCCACAGA ATTAGTATTGACAAGAAAATAACGGTAAGCAACATTATTTATGAGGCTATGTTTCAAGAA GGTGCCTACTTAATCCGCGACTACTTATTTTATATTAGCTCCTTCATTGGATGTGCTATT TATGCTAGACATCTTCCCGGATTGGTCAATTTCTGTATTTTGTCTACATTTATGCTAGTT TTCGACTTGCTTTTGTCTGCTACTTTTTATTCTGCCATTTTATCAATGAAGCTGGAAATT AACATCATTCACAGATCAACCGTCATCAGACAGACTTTGGAAGAGGACGGAGTTGTCCCA ACTACAGCAGATATTATATATAAGGATGAAACTGCCTCAGAACCACATTTTTTGAGATCT AACGTGGCTATCATTCTGGGAAAAGCATCAGTTATTGGTCTTTTGCTTCTGATCAACCTT TATGTTTTCACAGATAAGTTAAATGCTACAATACTAAACACGGTATATTTTGACTCTACA ATTTACTCGTTACCAAATTTTATCAATTATAAAGATATTGGCAATCTCAGCAATCAAGTG ATCATTTCCGTGTTGCCAAAGCAATATTATACTCCGCTGAAAAAATACCATCAGATCGAA GATTCTGTTCTACTTATCATTGATTCCGTTAGCAATGCTATTCGGGACCAATTTATCAGC AAGTTACTTTTTTTTGCATTTGCAGTTAGTATTTCCATCAATGTCTACTTACTGAATGCT GCAAAAATTCACACAGGATACATGAACTTCCAACCACAATCAAATAAGATCGATGATCTT GTTGTTCAGCAAAAATCGGCAACGATTGAGTTTTCAGAAACTCGAAGTATGCCTGCTTCT TCTGGCCTAGAAACTCCAGTGACCGCGAAAGATATAATTATCTCTGAAGAAATCCAGAAT AACGAATGCGTCTATGCTTTGAGTTCCCAGGACGAGCCTATCCGTCCTTTATCGAATTTA GTGGAACTTATGGAGAAAGAACAATTAAAGAACATGAATAATACTGAGGTTTCGAATCTT GTCGTCAACGGTAAACTGCCATTATATTCCTTAGAGAAAAAATTAGAGGACACAACTCGT GCGGTTTTAGTTAGGAGAAAGGCACTTTCAACTTTGGCTGAATCGCCAATTTTAGTTTCC GAAAAATTGCCCTTCAGAAATTATGATTATGATCGCGTTTTTGGAGCTTGCTGTGAAAAT GTCATCGGCTATATGCCAATACCAGTTGGTGTAATTGGTCCATTAATTATTGATGGAACA TCTTATCACATACCAATGGCAACCACGGAAGGTTGTTTAGTGGCTTCAGCTATGCGTGGT TGCAAAGCCATCAATGCTGGTGGTGGTGCAACAACTGTTTTAACCAAAGATGGTATGACT AGAGGCCCAGTCGTTCGTTTCCCTACTTTAATAAGATCTGGTGCCTGCAAGATATGGTTA GACTCGGAAGAGGGACAAAATTCAATTAAAAAAGCTTTTAATTCTACATCAAGGTTTGCA CGTTTGCAACATATTCAAACCTGTCTAGCAGGCGATTTGCTTTTTATGAGATTTCGGACA ACTACCGGTGACGCAATGGGTATGAACATGATATCGAAAGGTGTCGAATACTCTTTGAAA CAAATGGTAGAAGAATATGGTTGGGAAGATATGGAAGTTGTCTCCGTATCTGGTAACTAT TGTACTGATAAGAAACCTGCCGCAATCAATTGGATTGAAGGTCGTGGTAAAAGTGTCGTA GCTGAAGCTACTATTCCTGGTGATGTCGTAAAAAGTGTTTTAAAGAGCGATGTTTCCGCT TTAGTTGAATTAAATATATCCAAGAACTTGGTTGGATCCGCAATGGCTGGATCTGTTGGT GGTTTCAACGCGCACGCAGCTAATTTGGTCACTGCACTTTTCTTGGCATTAGGCCAAGAT CCTGCGCAGAACGTCGAAAGTTCCAACTGTATAACTTTGATGAAGGAAGTTGATGGTGAT TTAAGGATCTCTGTTTCCATGCCATCTATTGAAGTTGGTACGATTGGCGGGGGTACTGTT CTGGAGCCTCAGGGCGCCATGCTTGATCTTCTCGGCGTTCGTGGTCCTCACCCCACTGAA CCTGGAGCAAATGCTAGGCAATTAGCTAGAATAATCGCGTGTGCTGTCTTGGCTGGTGAA CTGTCTCTGTGCTCCGCACTTGCTGCCGGTCACCTGGTACAAAGCCATATGACTCACAAC CGTAAAACAAACAAAGCCAATGAACTGCCACAACCAAGTAACAAAGGGCCCCCCTGTAAA ACCTCAGCATTATTATAA
Protein Properties
Pfam Domain Function
Protein Residues1045
Protein Molecular Weight115691.0
Protein Theoretical pI7.62
Signalling Regions
  • None
Transmembrane Regions
  • 27-53
  • 186-210
  • 241-265
  • 299-323
  • 331-356
  • 397-421
  • 498-523
Protein Sequence>3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 MSLPLKTIVHLVKPFACTARFSARYPIHVIVVAVLLSAAAYLSVTQSYLNEWKLDSNQYS TYLSIKPDELFEKCTHYYRSPVSDTWKLLSSKEAADIYTPFHYYLSTISFQSKDNSTTLP SLDDVIYSVDHTRYLLSEEPKIPTELVSENGTKWRLRNNSNFILDLHNIYRNMVKQFSNK TSEFDQFDLFIILAAYLTLFYTLCCLFNDMRKIGSKFWLSFSALSNSACALYLSLYTTHS LLKKPASLLSLVIGLPFIVVIIGFKHKVRLAAFSLQKFHRISIDKKITVSNIIYEAMFQE GAYLIRDYLFYISSFIGCAIYARHLPGLVNFCILSTFMLVFDLLLSATFYSAILSMKLEI NIIHRSTVIRQTLEEDGVVPTTADIIYKDETASEPHFLRSNVAIILGKASVIGLLLLINL YVFTDKLNATILNTVYFDSTIYSLPNFINYKDIGNLSNQVIISVLPKQYYTPLKKYHQIE DSVLLIIDSVSNAIRDQFISKLLFFAFAVSISINVYLLNAAKIHTGYMNFQPQSNKIDDL VVQQKSATIEFSETRSMPASSGLETPVTAKDIIISEEIQNNECVYALSSQDEPIRPLSNL VELMEKEQLKNMNNTEVSNLVVNGKLPLYSLEKKLEDTTRAVLVRRKALSTLAESPILVS EKLPFRNYDYDRVFGACCENVIGYMPIPVGVIGPLIIDGTSYHIPMATTEGCLVASAMRG CKAINAGGGATTVLTKDGMTRGPVVRFPTLIRSGACKIWLDSEEGQNSIKKAFNSTSRFA RLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNY CTDKKPAAINWIEGRGKSVVAEATIPGDVVKSVLKSDVSALVELNISKNLVGSAMAGSVG GFNAHAANLVTALFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTV LEPQGAMLDLLGVRGPHPTEPGANARQLARIIACAVLAGELSLCSALAAGHLVQSHMTHN RKTNKANELPQPSNKGPPCKTSALL
References
External Links
ResourceLink
Saccharomyces Genome Database HMG2
Uniprot IDP12684
Uniprot NameHMDH2_YEAST
GenBank Gene IDM22255
Genebank Protein ID171688
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
  • 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
  • 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
  • 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
  • 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