A0A1D8PC43 · MVD1_CANAL
- ProteinDiphosphomevalonate decarboxylase
- GeneMVD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids362 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Diphosphomevalonate decarboxylase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:12073030).
MVD1 converts diphosphomevalonate into isopentenyl diphosphate (PubMed:12073030).
The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable)
MVD1 converts diphosphomevalonate into isopentenyl diphosphate (PubMed:12073030).
The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable)
Catalytic activity
- (R)-5-diphosphomevalonate + ATP = isopentenyl diphosphate + ADP + phosphate + CO2This reaction proceeds in the forward direction.
Pathway
Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 3/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 17-20 | (R)-5-diphosphomevalonate (UniProtKB | ChEBI) | |||
Binding site | 72 | (R)-5-diphosphomevalonate (UniProtKB | ChEBI) | |||
Binding site | 150-155 | (R)-5-diphosphomevalonate (UniProtKB | ChEBI) | |||
Binding site | 206 | (R)-5-diphosphomevalonate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | diphosphomevalonate decarboxylase activity | |
Biological Process | isopentenyl diphosphate biosynthetic process, mevalonate pathway | |
Biological Process | sterol biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDiphosphomevalonate decarboxylase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida
Accessions
- Primary accessionA0A1D8PC43
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000454168 | 1-362 | Diphosphomevalonate decarboxylase | ||
Expression
Induction
Expression is high in media supplemented with glucose, moderate in acetate, galactose and low in maltose medium (PubMed:12073030).
Expression is higher in the yeast phase than in the hyphal phase of growth as well as higher in the exponential than in the stationary phase (PubMed:12073030).
Expression is affected by antifungals (PubMed:15917516).
Expression is repressed during biofilm formation (PubMed:19527170, PubMed:22265407).
Expression is higher in the yeast phase than in the hyphal phase of growth as well as higher in the exponential than in the stationary phase (PubMed:12073030).
Expression is affected by antifungals (PubMed:15917516).
Expression is repressed during biofilm formation (PubMed:19527170, PubMed:22265407).
Interaction
Structure
Sequence
- Sequence statusComplete
- Length362
- Mass (Da)39,544
- Last updated2017-01-18 v1
- MD5 Checksum1DC0A407A26CB1687F646C8655AB1CBA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP017623 EMBL· GenBank· DDBJ | AOW25709.1 EMBL· GenBank· DDBJ | Genomic DNA |