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P17256 (KIME_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm. Peroxisome.

Involvement in disease

Note=Mutation in the mevalonate kinase gene causes mevalonicaciduria.

Sequence similarities

Belongs to the GHMP kinase family. Mevalonate kinase subfamily.

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...

Sequences

Sequence LengthMass (Da)Tools
P17256 [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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M29472 mRNA. Translation: AAA41588.1.
IPIIPI00214563.
PIRA35629.
RefSeqNP_112325.1. NM_031063.1.
UniGeneRn.6995.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KVKX-ray2.40A1-395[»]
2R42X-ray2.40A1-395[»]
ProteinModelPortalP17256.
SMRP17256. Positions 1-395.
ModBaseSearch...

PTM databases

PhosphoSiteP17256.

Proteomic databases

PRIDEP17256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81727.
KEGGrno:81727.

Organism-specific databases

CTD4598.
RGD621295. Mvk.

Phylogenomic databases

HOVERGENHBG000402.
PhylomeDBP17256.

Gene expression databases

GenevestigatorP17256.

Family and domain databases

InterProIPR006204. GHMP_kinase.
IPR013750. GHMP_kinase_C.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR006205. Mev_gal_kin.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
KOK00869.
PfamPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PRINTSPR00959. MEVGALKINASE.
SUPFAMSSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
TIGRFAMsTIGR00549. Mevalon_kin. 1 hit.
PROSITEPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615384.

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: November 16, 2011
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

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