MVD1/YNR043W Summary Help

Standard Name MVD1 1
Systematic Name YNR043W
Alias ERG19 2
Feature Type ORF, Verified
Description Mevalonate pyrophosphate decarboxylase; essential enzyme involved in the biosynthesis of isoprenoids and sterols, including ergosterol; acts as a homodimer (2, 3, 4 and see Summary Paragraph)
Name Description MeValonate pyrophosphate Decarboxylase
Chromosomal Location
ChrXIV:701895 to 703085 | ORF Map | GBrowse
Gene Ontology Annotations All MVD1 GO evidence and references
  View Computational GO annotations for MVD1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 5 genes
Classical genetics
Large-scale survey
reduction of function
34 total interaction(s) for 31 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 11
  • Affinity Capture-RNA: 2

Genetic Interactions
  • Negative Genetic: 14
  • Positive Genetic: 5
  • Synthetic Growth Defect: 2

Expression Summary
Length (a.a.) 396
Molecular Weight (Da) 44,115
Isoelectric Point (pI) 5.56
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIV:701895 to 703085 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1191 701895..703085 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005326

MVD1 encodes diphosphomevalonate decarboxylase, which converts mevalonate-5-pyrophosphate to isopentenyl pyrophosphate in the biosynthesis of isoprenoids and sterols, including ergosterol in yeast (2, 5, 6). MVD1 is essential for viability; a temperature-sensitive mvd1 mutation is auxotrophic for ergosterol and lacks diphosphomevalonate decarboxylase activity (2, 4). Mvd1p acts as a homodimer; the temperature-sensitive erg19-34 allele impairs dimerization (3).

Mvd1p is a member of the GHMP kinase superfamily, which includes small-molecule kinases such as galactokinase, homoserine kinase, mevalonate kinase, and phosphomevalonate kinase (7, 8). The human diphosphomevalonate decarboxylase has been cloned and sequenced, and is a possible target in the treatment of hypercholesterolemia (5). The Arabidopsis enzyme, encoded by AtMVD1, complements S. cerevisiae mvd1 mutant phenotypes (9).

Last updated: 2009-07-29 Contact SGD

References cited on this page View Complete Literature Guide for MVD1
1) SGD  (2009) Gene name standardized from a GenBank/EMBL/DDBJ record
2) Chambon C, et al.  (1991) Sterol pathway in yeast. Identification and properties of mutant strains defective in mevalonate diphosphate decarboxylase and farnesyl diphosphate synthetase. Lipids 26(8):633-6
3) Cordier H, et al.  (1999) The Saccharomyces cerevisiae mevalonate diphosphate decarboxylase (erg19p) forms homodimers in vivo, and a single substitution in a structurally conserved region impairs dimerization. Curr Microbiol 38(5):290-4
4) Berges T, et al.  (1997) The Saccharomyces cerevisiae mevalonate diphosphate decarboxylase is essential for viability, and a single Leu-to-Pro mutation in a conserved sequence leads to thermosensitivity. J Bacteriol 179(15):4664-70
5) Toth MJ and Huwyler L  (1996) Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase. J Biol Chem 271(14):7895-8
6) Parks LW, et al.  (1995) Biochemical and physiological effects of sterol alterations in yeast--a review. Lipids 30(3):227-30
7) Bonanno JB, et al.  (2001) Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis. Proc Natl Acad Sci U S A 98(23):12896-901
8) Krepkiy DV and Miziorko HM  (2005) Investigation of the functional contributions of invariant serine residues in yeast mevalonate diphosphate decarboxylase. Biochemistry 44(7):2671-7
9) Cordier H, et al.  (1999) Heterologous expression in Saccharomyces cerevisiae of an Arabidopsis thaliana cDNA encoding mevalonate diphosphate decarboxylase. Plant Mol Biol 39(5):953-67