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Protein

Diphosphomevalonate decarboxylase

Gene

MVD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

Present with 13700 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2.

Pathwayi: isopentenyl diphosphate biosynthesis via mevalonate pathway

This protein is involved in step 3 of the subpathway that synthesizes isopentenyl diphosphate from (R)-mevalonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Mevalonate kinase (ERG12)
  2. Phosphomevalonate kinase (ERG8)
  3. Diphosphomevalonate decarboxylase (MVD1)
This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via mevalonate pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from (R)-mevalonate, the pathway isopentenyl diphosphate biosynthesis via mevalonate pathway and in Isoprenoid biosynthesis.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • diphosphomevalonate decarboxylase activity Source: SGD

GO - Biological processi

  • isopentenyl diphosphate biosynthetic process, mevalonate pathway Source: GO_Central
  • sterol biosynthetic process Source: SGD

Keywordsi

Molecular functionLyase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-653
YEAST:MONOMER-653
YEAST:YNR043W-MONOMER
BRENDAi4.1.1.33 984
ReactomeiR-SCE-191273 Cholesterol biosynthesis
R-SCE-446199 Synthesis of Dolichyl-phosphate
SABIO-RKiP32377
UniPathwayiUPA00057; UER00100

Names & Taxonomyi

Protein namesi
Recommended name:
Diphosphomevalonate decarboxylase (EC:4.1.1.33)
Alternative name(s):
Ergosterol biosynthesis protein 19
Mevalonate pyrophosphate decarboxylase
Mevalonate-5-diphosphate decarboxylase
Short name:
MDD
Short name:
MDDase
Gene namesi
Name:MVD1
Synonyms:ERG19, MPD
Ordered Locus Names:YNR043W
ORF Names:N3427
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNR043W
SGDiS000005326 MVD1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000870151 – 396Diphosphomevalonate decarboxylaseAdd BLAST396

Proteomic databases

MaxQBiP32377
PaxDbiP32377
PRIDEiP32377

PTM databases

iPTMnetiP32377

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi35868, 263 interactors
DIPiDIP-6729N
IntActiP32377, 2 interactors
MINTiP32377
STRINGi4932.YNR043W

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi13 – 17Combined sources5
Beta strandi22 – 24Combined sources3
Turni25 – 28Combined sources4
Beta strandi29 – 32Combined sources4
Beta strandi34 – 39Combined sources6
Turni41 – 43Combined sources3
Beta strandi46 – 52Combined sources7
Turni62 – 64Combined sources3
Beta strandi67 – 74Combined sources8
Helixi75 – 90Combined sources16
Helixi99 – 101Combined sources3
Beta strandi104 – 110Combined sources7
Helixi120 – 135Combined sources16
Helixi142 – 153Combined sources12
Helixi154 – 160Combined sources7
Beta strandi161 – 168Combined sources8
Beta strandi179 – 184Combined sources6
Helixi186 – 188Combined sources3
Beta strandi192 – 199Combined sources8
Helixi208 – 218Combined sources11
Helixi221 – 227Combined sources7
Helixi229 – 242Combined sources14
Helixi246 – 265Combined sources20
Beta strandi267 – 269Combined sources3
Helixi276 – 292Combined sources17
Beta strandi297 – 301Combined sources5
Beta strandi303 – 305Combined sources3
Beta strandi307 – 312Combined sources6
Helixi313 – 315Combined sources3
Helixi316 – 327Combined sources12
Turni334 – 336Combined sources3
Helixi339 – 350Combined sources12
Helixi363 – 366Combined sources4
Beta strandi367 – 375Combined sources9
Beta strandi389 – 391Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FI4X-ray2.27A1-396[»]
ProteinModelPortaliP32377
SMRiP32377
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32377

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000015359
InParanoidiP32377
KOiK01597
OMAiLTLHAMM
OrthoDBiEOG092C4EMB

Family and domain databases

Gene3Di3.30.230.10, 1 hit
3.30.70.890, 1 hit
InterProiView protein in InterPro
IPR036554 GHMP_kinase_C_sf
IPR006204 GHMP_kinase_N_dom
IPR005935 Mev_decarb
IPR029765 Mev_diP_decarb
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
PfamiView protein in Pfam
PF00288 GHMP_kinases_N, 1 hit
PIRSFiPIRSF015950 Mev_P_decrbx, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55060 SSF55060, 1 hit
TIGRFAMsiTIGR01240 mevDPdecarb, 1 hit

Sequencei

Sequence statusi: Complete.

P32377-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVYTASVTA PVNIATLKYW GKRDTKLNLP TNSSISVTLS QDDLRTLTSA
60 70 80 90 100
ATAPEFERDT LWLNGEPHSI DNERTQNCLR DLRQLRKEME SKDASLPTLS
110 120 130 140 150
QWKLHIVSEN NFPTAAGLAS SAAGFAALVS AIAKLYQLPQ STSEISRIAR
160 170 180 190 200
KGSGSACRSL FGGYVAWEMG KAEDGHDSMA VQIADSSDWP QMKACVLVVS
210 220 230 240 250
DIKKDVSSTQ GMQLTVATSE LFKERIEHVV PKRFEVMRKA IVEKDFATFA
260 270 280 290 300
KETMMDSNSF HATCLDSFPP IFYMNDTSKR IISWCHTINQ FYGETIVAYT
310 320 330 340 350
FDAGPNAVLY YLAENESKLF AFIYKLFGSV PGWDKKFTTE QLEAFNHQFE
360 370 380 390
SSNFTARELD LELQKDVARV ILTQVGSGPQ ETNESLIDAK TGLPKE
Length:396
Mass (Da):44,116
Last modified:October 1, 1996 - v2
Checksum:i6DDFCC72F1BB6430
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160L → S in AAT93171 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49261 mRNA Translation: AAC49252.1
X97557 Genomic DNA Translation: CAA66158.1
Z71658 Genomic DNA Translation: CAA96324.1
AY693152 Genomic DNA Translation: AAT93171.1
M81698 Genomic DNA Translation: AAA34506.2
BK006947 Genomic DNA Translation: DAA10584.1
PIRiS63374
RefSeqiNP_014441.1, NM_001183220.1

Genome annotation databases

EnsemblFungiiYNR043W; YNR043W; YNR043W
GeneIDi855779
KEGGisce:YNR043W

Similar proteinsi

Entry informationi

Entry nameiMVD1_YEAST
AccessioniPrimary (citable) accession number: P32377
Secondary accession number(s): D6W1L8, Q6B1C8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 165 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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