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Protein

Diphosphomevalonate decarboxylase

Gene

Mvd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Performs the first committed step in the biosynthesis of isoprenes.

Catalytic activityi

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

Pathwayi: cholesterol biosynthesis

This protein is involved in the pathway cholesterol biosynthesis, which is part of Steroid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway cholesterol biosynthesis and in Steroid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-191273. Cholesterol biosynthesis.
R-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-446199. Synthesis of Dolichyl-phosphate.
UniPathwayiUPA00063.

Names & Taxonomyi

Protein namesi
Recommended name:
Diphosphomevalonate decarboxylase (EC:4.1.1.33)
Alternative name(s):
Mevalonate (diphospho)decarboxylase
Short name:
MDDase
Mevalonate pyrophosphate decarboxylase
Gene namesi
Name:Mvd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2179327. Mvd.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 401400Diphosphomevalonate decarboxylasePRO_0000087013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99JF5.
MaxQBiQ99JF5.
PaxDbiQ99JF5.
PRIDEiQ99JF5.

PTM databases

iPTMnetiQ99JF5.
PhosphoSiteiQ99JF5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000006517.
CleanExiMM_MVD.
ExpressionAtlasiQ99JF5. baseline and differential.
GenevisibleiQ99JF5. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000006692.

Structurei

Secondary structure

1
401
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 157Combined sources
Beta strandi18 – 225Combined sources
Beta strandi27 – 293Combined sources
Turni30 – 334Combined sources
Beta strandi34 – 374Combined sources
Beta strandi39 – 446Combined sources
Turni46 – 483Combined sources
Beta strandi51 – 577Combined sources
Beta strandi65 – 684Combined sources
Beta strandi71 – 733Combined sources
Helixi78 – 9215Combined sources
Helixi103 – 1086Combined sources
Beta strandi111 – 1177Combined sources
Helixi121 – 1233Combined sources
Helixi127 – 14317Combined sources
Helixi150 – 1567Combined sources
Helixi158 – 1647Combined sources
Beta strandi165 – 1717Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi196 – 2049Combined sources
Helixi212 – 22211Combined sources
Helixi224 – 2329Combined sources
Helixi234 – 24613Combined sources
Helixi250 – 26920Combined sources
Beta strandi271 – 2733Combined sources
Helixi280 – 29617Combined sources
Beta strandi301 – 3044Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi311 – 3166Combined sources
Helixi317 – 3193Combined sources
Helixi320 – 33011Combined sources
Beta strandi341 – 3444Combined sources
Helixi353 – 3586Combined sources
Beta strandi367 – 37610Combined sources
Beta strandi381 – 3833Combined sources
Helixi386 – 3883Combined sources
Beta strandi395 – 3973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F0NX-ray1.90A/B6-401[»]
ProteinModelPortaliQ99JF5.
SMRiQ99JF5. Positions 8-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99JF5.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 544Poly-Thr

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2833. Eukaryota.
COG3407. LUCA.
GeneTreeiENSGT00390000015359.
HOVERGENiHBG051503.
InParanoidiQ99JF5.
KOiK01597.
OMAiCTDSNQF.
OrthoDBiEOG091G0EUU.
PhylomeDBiQ99JF5.
TreeFamiTF105952.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
InterProiIPR013750. GHMP_kinase_C_dom.
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.
[Graphical view]
PANTHERiPTHR10977. PTHR10977. 1 hit.
PfamiPF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFiPIRSF015950. Mev_P_decrbx. 1 hit.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR01240. mevDPdecarb. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99JF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEKPQDLM VTCTAPVNIA VIKYWGKRDE ALILPINSSL SVTLHQDQLK
60 70 80 90 100
TTTTVAISKD FTEDRIWLNG REEDVGQPRL QACLREIRRL ARKRRSTEDG
110 120 130 140 150
DTLPLSLSYK VHVASVNNFP TAAGLASSAA GYACLAYTLA QVYGVEGDLS
160 170 180 190 200
EVARRGSGSA CRSLYGGFVE WQMGEQADGK DSIARQIAPE WHWPQLRILI
210 220 230 240 250
LVVSADKKQT GSTVGMQTSV ETSTLLKFRA ESVVPERMKE MTRCIQEQDF
260 270 280 290 300
QGFAQLTMKD SNQFHATCLD TFPPISYLND TSRRIIQLVH RFNTHQGQTK
310 320 330 340 350
VAYTFDAGPN AVIFTLEDTV AEFVAAVRHS FPPAANGDKF LKGLQVAPVL
360 370 380 390 400
LSDELKAALA VEPSPGGVQY IIATQVGPGP QVLDDTHDHL LGQDGLPQRD

L
Length:401
Mass (Da):44,072
Last modified:November 13, 2007 - v2
Checksum:iBDF58921709C55AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291R → Q in BAE32901 (PubMed:16141072).Curated
Sequence conflicti229 – 2291R → Q in BAC40852 (PubMed:16141072).Curated
Sequence conflicti233 – 2331V → G in CAC35731 (Ref. 1) Curated
Sequence conflicti254 – 2541A → G in CAC35731 (Ref. 1) Curated
Sequence conflicti266 – 2661A → V in BAE32901 (PubMed:16141072).Curated
Sequence conflicti266 – 2661A → V in BAC40852 (PubMed:16141072).Curated
Sequence conflicti296 – 2961Q → H in BAE42019 (PubMed:16141072).Curated
Sequence conflicti296 – 2961Q → H in AAH08526 (PubMed:15489334).Curated
Sequence conflicti360 – 3601A → V in AAH08526 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ309922 mRNA. Translation: CAC35731.1.
AK089354 mRNA. Translation: BAC40852.1.
AK154883 mRNA. Translation: BAE32901.1.
AK170773 mRNA. Translation: BAE42019.1.
BC008526 mRNA. Translation: AAH08526.1.
CCDSiCCDS22738.1.
RefSeqiNP_619597.2. NM_138656.2.
UniGeneiMm.28146.

Genome annotation databases

EnsembliENSMUST00000006692; ENSMUSP00000006692; ENSMUSG00000006517.
GeneIDi192156.
KEGGimmu:192156.
UCSCiuc009nss.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ309922 mRNA. Translation: CAC35731.1.
AK089354 mRNA. Translation: BAC40852.1.
AK154883 mRNA. Translation: BAE32901.1.
AK170773 mRNA. Translation: BAE42019.1.
BC008526 mRNA. Translation: AAH08526.1.
CCDSiCCDS22738.1.
RefSeqiNP_619597.2. NM_138656.2.
UniGeneiMm.28146.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3F0NX-ray1.90A/B6-401[»]
ProteinModelPortaliQ99JF5.
SMRiQ99JF5. Positions 8-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000006692.

PTM databases

iPTMnetiQ99JF5.
PhosphoSiteiQ99JF5.

Proteomic databases

EPDiQ99JF5.
MaxQBiQ99JF5.
PaxDbiQ99JF5.
PRIDEiQ99JF5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006692; ENSMUSP00000006692; ENSMUSG00000006517.
GeneIDi192156.
KEGGimmu:192156.
UCSCiuc009nss.2. mouse.

Organism-specific databases

CTDi4597.
MGIiMGI:2179327. Mvd.

Phylogenomic databases

eggNOGiKOG2833. Eukaryota.
COG3407. LUCA.
GeneTreeiENSGT00390000015359.
HOVERGENiHBG051503.
InParanoidiQ99JF5.
KOiK01597.
OMAiCTDSNQF.
OrthoDBiEOG091G0EUU.
PhylomeDBiQ99JF5.
TreeFamiTF105952.

Enzyme and pathway databases

UniPathwayiUPA00063.
ReactomeiR-MMU-191273. Cholesterol biosynthesis.
R-MMU-2426168. Activation of gene expression by SREBF (SREBP).
R-MMU-446199. Synthesis of Dolichyl-phosphate.

Miscellaneous databases

EvolutionaryTraceiQ99JF5.
PROiQ99JF5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000006517.
CleanExiMM_MVD.
ExpressionAtlasiQ99JF5. baseline and differential.
GenevisibleiQ99JF5. MM.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
InterProiIPR013750. GHMP_kinase_C_dom.
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.
[Graphical view]
PANTHERiPTHR10977. PTHR10977. 1 hit.
PfamiPF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PIRSFiPIRSF015950. Mev_P_decrbx. 1 hit.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR01240. mevDPdecarb. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMVD1_MOUSE
AccessioniPrimary (citable) accession number: Q99JF5
Secondary accession number(s): Q3TCD8, Q8BTM4, Q922D7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 13, 2007
Last modified: September 7, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.