3-hydroxy-3-methylglutaryl-coenzyme A reductase
Details
- Name
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Synonyms
- 1.1.1.88
- HMG-CoA reductase
- Gene Name
- mvaA
- Organism
- Pseudomonas mevalonii
- Amino acid sequence
>lcl|BSEQ0011332|3-hydroxy-3-methylglutaryl-coenzyme A reductase MSLDSRLPAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIENVIGTFEL PYAVASNFQINGRDVLVPLVVEEPSIVAAASYMAKLARANGGFTTSSSAPLMHAQVQIVG IQDPLNARLSLLRRKDEIIELANRKDQLLNSLGGGCRDIEVHTFADTPRGPMLVAHLIVD VRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFS GEAVIEGILDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGH YGSLTTWEKDNNGHLVGTLEMPMPVGLVGGATKTHPLAQLSLRILGVKTAQALAEIAVAV GLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWVARQLVEYHDVRADRAVA LLKQKRGQ
- Number of residues
- 428
- Molecular Weight
- 45589.915
- Theoretical pI
- 6.71
- GO Classification
- Functionscoenzyme binding / hydroxymethylglutaryl-CoA reductase (NADPH) activity / hydroxymethylglutaryl-CoA reductase activityProcessescoenzyme A metabolic process
- General Function
- Hydroxymethylglutaryl-coa reductase activity
- Specific Function
- P.mevalonii can use mevalonate as sole carbon source. With this enzyme mevalonate is deacetylated to HMG-CoA.
- Pfam Domain Function
- HMG-CoA_red (PF00368)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0003676|1287 bp ATGAGCCTCGATTCCCGCCTGCCCGCTTTCCGTAACCTGTCCCCTGCCGCGCGCCTGGAC CACATCGGCCAGTTGCTCGGCCTGAGCCACGACGATGTCAGCCTGCTGGCCAACGCCGGT GCCCTGCCGATGGACATCGCCAACGGCATGATCGAAAACGTCATCGGCACCTTCGAGCTG CCCTATGCCGTGGCCAGCAACTTCCAGATCAATGGCCGTGATGTGCTGGTGCCGCTGGTG GTGGAAGAGCCCTCGATCGTCGCCGCTGCTTCGTACATGGCCAAGCTGGCCCGTGCCAAC GGCGGCTTCACCACCTCCAGCAGCGCCCCGCTGATGCATGCCCAGGTACAGATCGTCGGC ATACAGGACCCGCTCAATGCACGCCTGAGCCTGCTGCGCCGCAAAGACGAAATCATTGAA CTGGCCAACCGCAAGGACCAGTTGCTCAACAGCCTCGGCGGCGGCTGCCGCGACATCGAA GTGCACACCTTCGCCGATACCCCGCGTGGCCCGATGCTGGTGGCGCACCTGATCGTCGAT GTACGCGATGCCATGGGCGCCAACACCGTCAATACCATGGCCGAGGCCGTTGCGCCGCTG ATGGAAGCCATCACCGGGGGCCAGGTACGCCTGCGCATTCTGTCCAACCTGGCCGACCTG CGCCTGGCCAGGGCCCAGGTGCGGATTACTCCGCAGCAACTGGAAACGGCCGAATTCAGT GGCGAGGCAGTGATCGAAGGCATCCTCGACGCCTACGCCTTCGCTGCGGTCGACCCTTAC CGCGCGGCCACCCACAACAAGGGCATCATGAATGGCATCGACCCACTGATCGTCGCCACT GGCAACGACTGGCGTGCAGTGGAAGCCGGCGCCCATGCGTATGCCTGCCGCAGTGGTCAC TACGGCTCGCTGACCACCTGGGAAAAGGACAACAACGGCCATTTGGTCGGCACCCTGGAA ATGCCGATGCCCGTAGGCCTGGTCGGCGGCGCCACCAAAACCCATCCGCTGGCGCAACTG TCGCTGCGCATCCTCGGCGTGAAAACAGCCCAGGCGCTCGCTGAGATTGCCGTGGCCGTA GGCCTGGCGCAAAACCTCGGGGCCATGCGCGCCCTGGCCACCGAAGGCATCCAGCGCGGC CACATGGCCCTGCATGCGCGCAATATTGCCGTGGTGGCGGGCGCCCGAGGCGATGAGGTG GACTGGGTTGCCCGGCAGTTGGTGGAATACCACGACGTGCGCGCCGACCGCGCCGTAGCA CTGCTGAAACAAAAGCGCGGCCAATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P13702 UniProtKB Entry Name MVAA_PSEMV GenBank Protein ID 151259 GenBank Gene ID M24015 - General References
- Beach MJ, Rodwell VW: Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Bacteriol. 1989 Jun;171(6):2994-3001. [Article]
- Wang YL, Beach MJ, Rodwell VW: (S)-3-hydroxy-3-methylglutaryl coenzyme A reductase, a product of the mva operon of Pseudomonas mevalonii, is regulated at the transcriptional level. J Bacteriol. 1989 Oct;171(10):5567-71. [Article]
- Wang Y, Darnay BG, Rodwell VW: Identification of the principal catalytically important acidic residue of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem. 1990 Dec 15;265(35):21634-41. [Article]
- Darnay BG, Wang Y, Rodwell VW: Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J Biol Chem. 1992 Jul 25;267(21):15064-70. [Article]
- Tabernero L, Bochar DA, Rodwell VW, Stauffacher CV: Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci U S A. 1999 Jun 22;96(13):7167-71. [Article]