KIME_BOVIN
ID KIME_BOVIN Reviewed; 396 AA.
AC Q5E9T8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Mevalonate kinase {ECO:0000305};
DE Short=MK;
DE EC=2.7.1.36 {ECO:0000250|UniProtKB:Q03426};
GN Name=MVK {ECO:0000250|UniProtKB:Q03426};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5-
CC phosphate, a key step in isoprenoid and cholesterol biosynthesis.
CC {ECO:0000250|UniProtKB:Q03426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+);
CC Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216;
CC EC=2.7.1.36; Evidence={ECO:0000250|UniProtKB:Q03426};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P17256};
CC -!- ACTIVITY REGULATION: Farnesyl pyrophosphate and geranyl pyrophosphate
CC inhibit mevalonate kinase activity by binding competitively at the ATP-
CC binding sites. {ECO:0000250|UniProtKB:Q03426}.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q03426}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17256}.
CC Peroxisome {ECO:0000250|UniProtKB:P17256}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT020832; AAX08849.1; -; mRNA.
DR EMBL; BC104540; AAI04541.1; -; mRNA.
DR RefSeq; NP_001015528.1; NM_001015528.1.
DR AlphaFoldDB; Q5E9T8; -.
DR SMR; Q5E9T8; -.
DR STRING; 9913.ENSBTAP00000006828; -.
DR PaxDb; Q5E9T8; -.
DR PRIDE; Q5E9T8; -.
DR Ensembl; ENSBTAT00000006828; ENSBTAP00000006828; ENSBTAG00000005183.
DR GeneID; 505792; -.
DR KEGG; bta:505792; -.
DR CTD; 4598; -.
DR VEuPathDB; HostDB:ENSBTAG00000005183; -.
DR VGNC; VGNC:31768; MVK.
DR eggNOG; KOG1511; Eukaryota.
DR GeneTree; ENSGT00950000183187; -.
DR InParanoid; Q5E9T8; -.
DR OMA; NTVCTYG; -.
DR OrthoDB; 1196330at2759; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000005183; Expressed in diaphragm and 107 other tissues.
DR ExpressionAtlas; Q5E9T8; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004496; F:mevalonate kinase activity; ISS:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43290; PTHR43290; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00549; mevalon_kin; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW Kinase; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Nucleotide-binding; Peroxisome; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..396
FT /note="Mevalonate kinase"
FT /id="PRO_0000282963"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q03426"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q03426"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 140..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P17256"
SQ SEQUENCE 396 AA; 42070 MW; ADF4A6D40DA5C4FA CRC64;
MLSEVLLVSA PGKVILHGEH AVVHGKVALA VALNLRTFLR LQPHSNGRVG LNLPNIGVRR
AWDVASLQLL DTSFLGHGDS AALTAKHVEK LKEVAGFPKD CVDPEHLAVL AFLYLYLSIC
QSQRALPSLD ITVWSELPTG AGLGSSAAYS VCLAAALLTA CEEIPNPLKD GEAAGRWTEE
NLELINKWAF QGERVIHGNP SGVDNAVSTW GGALRYQQGK ISSLKRPPVL KILLINTKVP
RSTKVLVANV RSRLLKFPEI VAPLLTSIDA ISLECERVLG EMAAAPTPEH YLTLEELIDM
NQHHLNALGV GHASLDQLCQ VTTAHGLHSK LTGAGGGGCG ITLLRPDVER PAVEATKRAL
SGCGFDCWET SVGAPGVSVH TAASLDASVQ QGLDSL
