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Protein

Diphosphomevalonate decarboxylase

Gene

Mvd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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

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

GO - Biological processi

  • cholesterol biosynthetic process Source: RGD
  • isopentenyl diphosphate biosynthetic process, mevalonate pathway Source: RGD
  • response to drug Source: RGD
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

BRENDAi4.1.1.33. 5301.
SABIO-RKQ62967.
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
Synonyms:Mpd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621292. Mvd.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • peroxisomal matrix Source: RGD
  • peroxisome Source: RGD
Complete GO annotation...

Pathology & Biotechi

Chemistry

GuidetoPHARMACOLOGYi642.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 401400Diphosphomevalonate decarboxylasePRO_0000087014Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ62967.
PRIDEiQ62967.

PTM databases

iPTMnetiQ62967.
PhosphoSiteiQ62967.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018145.

Structurei

3D structure databases

ProteinModelPortaliQ62967.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2833. Eukaryota.
COG3407. LUCA.
HOVERGENiHBG051503.
InParanoidiQ62967.
KOiK01597.
PhylomeDBiQ62967.

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.

Q62967-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEKPQDLM VTCTAPVNIA VIKYWGKRDE ALILPINPSL SVTLHQDQLK
60 70 80 90 100
TTTTAAISKD FTEDRIWLNG REEDVGQPRL QACLREIRRL ARKRRSTGDG
110 120 130 140 150
DALPLSLGYK VHVASVNNFP TAAGLASSAA GYACLAYTLA RVYGVEGDLS
160 170 180 190 200
EVARRGSGSA CRSLYGGFVE WQMGEQADGK DSIARQIAPE WHWPQLRVLI
210 220 230 240 250
LVVSAEKKPT GSTVGMQTSV ATSTLLKFRA ESIVPERMKE MTRCIQEQDF
260 270 280 290 300
QAFAQLTMKD SNQFHATCLD TFPPISYLND TSRRIIQLVH RFNAHHGQTK
310 320 330 340 350
VAYTFDAGPN AVIFTLEDTV AEFVAAVRHS FPPAANGDKF LKGLQVAPVL
360 370 380 390 400
LSDELKTSLA TEPSPGGVQY IIATQVGPGP QVLDDPHHHL LGPDGLPQRD

L
Length:401
Mass (Da):43,903
Last modified:November 1, 1997 - v1
Checksum:i6DC17437C170A645
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53706 mRNA. Translation: AAB00192.1.
RefSeqiNP_112324.1. NM_031062.2.
UniGeneiRn.10288.

Genome annotation databases

GeneIDi81726.
KEGGirno:81726.
UCSCiRGD:621292. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53706 mRNA. Translation: AAB00192.1.
RefSeqiNP_112324.1. NM_031062.2.
UniGeneiRn.10288.

3D structure databases

ProteinModelPortaliQ62967.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018145.

Chemistry

GuidetoPHARMACOLOGYi642.

PTM databases

iPTMnetiQ62967.
PhosphoSiteiQ62967.

Proteomic databases

PaxDbiQ62967.
PRIDEiQ62967.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81726.
KEGGirno:81726.
UCSCiRGD:621292. rat.

Organism-specific databases

CTDi4597.
RGDi621292. Mvd.

Phylogenomic databases

eggNOGiKOG2833. Eukaryota.
COG3407. LUCA.
HOVERGENiHBG051503.
InParanoidiQ62967.
KOiK01597.
PhylomeDBiQ62967.

Enzyme and pathway databases

UniPathwayiUPA00063.
BRENDAi4.1.1.33. 5301.
SABIO-RKQ62967.

Miscellaneous databases

PROiQ62967.

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_RAT
AccessioniPrimary (citable) accession number: Q62967
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.