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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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000870132 – 401Diphosphomevalonate decarboxylaseAdd BLAST400

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99JF5.
MaxQBiQ99JF5.
PaxDbiQ99JF5.
PRIDEiQ99JF5.

PTM databases

iPTMnetiQ99JF5.
PhosphoSitePlusiQ99JF5.

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

1401
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 15Combined sources7
Beta strandi18 – 22Combined sources5
Beta strandi27 – 29Combined sources3
Turni30 – 33Combined sources4
Beta strandi34 – 37Combined sources4
Beta strandi39 – 44Combined sources6
Turni46 – 48Combined sources3
Beta strandi51 – 57Combined sources7
Beta strandi65 – 68Combined sources4
Beta strandi71 – 73Combined sources3
Helixi78 – 92Combined sources15
Helixi103 – 108Combined sources6
Beta strandi111 – 117Combined sources7
Helixi121 – 123Combined sources3
Helixi127 – 143Combined sources17
Helixi150 – 156Combined sources7
Helixi158 – 164Combined sources7
Beta strandi165 – 171Combined sources7
Beta strandi184 – 188Combined sources5
Beta strandi196 – 204Combined sources9
Helixi212 – 222Combined sources11
Helixi224 – 232Combined sources9
Helixi234 – 246Combined sources13
Helixi250 – 269Combined sources20
Beta strandi271 – 273Combined sources3
Helixi280 – 296Combined sources17
Beta strandi301 – 304Combined sources4
Beta strandi307 – 309Combined sources3
Beta strandi311 – 316Combined sources6
Helixi317 – 319Combined sources3
Helixi320 – 330Combined sources11
Beta strandi341 – 344Combined sources4
Helixi353 – 358Combined sources6
Beta strandi367 – 376Combined sources10
Beta strandi381 – 383Combined sources3
Helixi386 – 388Combined sources3
Beta strandi395 – 397Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ99JF5.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi51 – 54Poly-Thr4

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)DescriptionActionsGraphical viewLength
Sequence conflicti229R → Q in BAE32901 (PubMed:16141072).Curated1
Sequence conflicti229R → Q in BAC40852 (PubMed:16141072).Curated1
Sequence conflicti233V → G in CAC35731 (Ref. 1) Curated1
Sequence conflicti254A → G in CAC35731 (Ref. 1) Curated1
Sequence conflicti266A → V in BAE32901 (PubMed:16141072).Curated1
Sequence conflicti266A → V in BAC40852 (PubMed:16141072).Curated1
Sequence conflicti296Q → H in BAE42019 (PubMed:16141072).Curated1
Sequence conflicti296Q → H in AAH08526 (PubMed:15489334).Curated1
Sequence conflicti360A → V in AAH08526 (PubMed:15489334).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3F0NX-ray1.90A/B6-401[»]
ProteinModelPortaliQ99JF5.
SMRiQ99JF5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000006692.

PTM databases

iPTMnetiQ99JF5.
PhosphoSitePlusiQ99JF5.

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: November 2, 2016
This is version 113 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.