Identification |
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Name | 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 |
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Synonyms | |
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Gene Name | HMG1 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in hydroxymethylglutaryl-CoA reductase (NADPH) activity |
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Specific Function | This transmembrane glycoprotein is involved in the control of cholesterol biosynthesis. It is the rate-limiting enzyme of the sterol biosynthesis |
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Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein |
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SMPDB Pathways |
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KEGG Pathways | Terpenoid backbone biosynthesis | ec00900 | |
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SMPDB Reactions | |
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KEGG Reactions | |
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Metabolites | YMDB ID | Name | View |
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YMDB00045 | Coenzyme A | Show | YMDB00310 | 22b-Hydroxycholesterol | Show | YMDB00426 | NADPH | Show | YMDB00427 | NADP | Show | YMDB00707 | (R)-Mevalonic acid | Show | YMDB00708 | 3-Hydroxy-3-methylglutaryl-CoA | Show | YMDB00862 | hydron | Show | YMDB01039 | (R)-Mevalonate | Show |
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GO Classification | Component |
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cell part | membrane part | intrinsic to membrane | integral to membrane | Function |
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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 | hydroxymethylglutaryl-CoA reductase (NADPH) activity | Process |
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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 |
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Gene Properties |
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Chromosome Location | chromosome 13 |
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Locus | YML075C |
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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 |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 1054 |
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Protein Molecular Weight | 115624.0 |
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Protein Theoretical pI | 8.09 |
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Signalling Regions | |
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Transmembrane Regions | - 27-53
- 187-211
- 242-266
- 300-324
- 332-357
- 398-422
- 499-524
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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 |
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References |
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External Links | |
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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
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