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Reviewed, UniProtKB/Swiss-Prot P17256 (KIME_RAT)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mevalonate kinase
      Short name=MK
    EC=2.7.1.36
Gene names
Name: Mvk
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

May be a regulatory site in cholesterol biosynthetic pathway.

Catalytic activity

ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate.

Enzyme regulation

Farnesyl- and geranyl-pyrophosphates are competitive inhibitors.

Pathway

Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via mevalonic acid pathway; isopentenyl-PP from (R)-mevalonic acid: step 1/3.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm. Peroxisome.

Involvement in disease

Mutation in the mevalonate kinase gene causes mevalonicaciduria.

Sequence similarities

Belongs to the GHMP kinase family. Mevalonate kinase subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Mevalonate kinase
PRO_0000156659

Regions

Nucleotide binding138 – 14811ATP

Sites

Binding site551ATP
Binding site1041ATP
Binding site1081ATP
Binding site1351ATP

Secondary structure

1 ............................................................ 395
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P17256-1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 803D1F44E3C525FC

FASTA39541,988
        10         20         30         40         50         60 
MLSEVLLVSA PGKVILHGEH AVVHGKVALA VALNLRTFLV LRPQSNGKVS LNLPNVGIKQ 

        70         80         90        100        110        120 
VWDVATLQLL DTGFLEQGDV PAPTLEQLEK LKKVAGLPRD CVGNEGLSLL AFLYLYLAIC 

       130        140        150        160        170        180 
RKQRTLPSLD IMVWSELPPG AGLGSSAAYS VCVAAALLTA CEEVTNPLKD RGSIGSWPEE 

       190        200        210        220        230        240 
DLKSINKWAY EGERVIHGNP SGVDNSVSTW GGALRYQQGK MSSLKRLPAL QILLTNTKVP 

       250        260        270        280        290        300 
RSTKALVAGV RSRLIKFPEI MAPLLTSIDA ISLECERVLG EMAAAPVPEQ YLVLEELMDM 

       310        320        330        340        350        360 
NQHHLNALGV GHASLDQLCQ VTAAHGLHSK LTGAGGGGCG ITLLKPGLER AKVEAAKQAL 

       370        380        390 
TGCGFDCWET SIGAPGVSMH SATSIEDPVR QALGL

« Hide

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References

[1]"Molecular cloning of mevalonate kinase and regulation of its mRNA levels in rat liver."
Tanaka R.D., Lee L.Y., Schafer B.L., Kratunis V.J., Mohler W.A., Robinson G.W., Mosley S.T.
Proc. Natl. Acad. Sci. U.S.A. 87:2872-2876(1990) [PubMed: 2158094] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20.
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"The structure of a binary complex between a mammalian mevalonate kinase and ATP: insights into the reaction mechanism and human inherited disease."
Fu Z., Wang M., Potter D., Miziorko H.M., Kim J.-J.
J. Biol. Chem. 277:18134-18142(2002) [PubMed: 11877411] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ATP, SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M29472 mRNA. Translation: AAA41588.1.
IPIIPI00214563.
PIRA35629.
RefSeqNP_112325.1.
UniGeneRn.6995

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KVKX-ray2.40A1-395[»]
2R42X-ray2.40A1-395[»]
ModBaseSearch...

Genome annotation databases

GeneID81727.
KEGGrno:81727.

Organism-specific databases

RGD621295. Mvk.

Phylogenomic databases

HOVERGENP17256.

Enzyme and pathway databases

BRENDA2.7.1.36. 248.

Family and domain databases

InterProIPR006204. GHMP_kinase.
IPR013750. GHMP_kinase_C.
IPR006203. GHMP_knse_ATP_bd_CS.
IPR006205. Mev_gal_kin.
IPR006206. Mev_galkinase.
IPR014721. Ribosomal_S5_D2-type_fold.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
PANTHERPTHR10457:SF4. Mev_gal_kin. 1 hit.
PfamPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PRINTSPR00959. MEVGALKINASE.
TIGRFAMsTIGR00549. mevalon_kin. 1 hit.
PROSITEPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615384.

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Entry information

Entry nameKIME_RAT
AccessionPrimary (citable) accession number: P17256
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents