Survey with prize
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Yeast Metabolome Database.
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
integral to membrane
cell part
membrane part
intrinsic to membrane
Function
hydroxymethylglutaryl-CoA reductase (NADPH) activity
binding
nucleotide binding
oxidoreductase activity
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
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
metabolic process
lipid metabolic process
cellular lipid metabolic process
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