ID   PMVK_BOVIN              Reviewed;         192 AA.
AC   Q2KIU2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Phosphomevalonate kinase;
DE            Short=PMKase;
DE            EC=2.7.4.2 {ECO:0000250|UniProtKB:Q15126};
GN   Name=PMVK;
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].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible ATP-dependent phosphorylation of
CC       mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key
CC       step in the mevalonic acid mediated biosynthesis of isopentenyl
CC       diphosphate and other polyisoprenoid metabolites.
CC       {ECO:0000250|UniProtKB:Q15126}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
CC         ADP; Xref=Rhea:RHEA:16341, ChEBI:CHEBI:30616, ChEBI:CHEBI:57557,
CC         ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.4.2;
CC         Evidence={ECO:0000250|UniProtKB:Q15126};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC         Evidence={ECO:0000250|UniProtKB:Q15126};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16343;
CC         Evidence={ECO:0000250|UniProtKB:Q15126};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 2/3. {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q15126}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q15126}.
CC   -!- CAUTION: Was originally thought to be located in the peroxisome.
CC       However, was later shown to be cytosolic.
CC       {ECO:0000250|UniProtKB:Q15126}.
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DR   EMBL; BC112509; AAI12510.1; -; mRNA.
DR   RefSeq; NP_001039616.1; NM_001046151.2.
DR   AlphaFoldDB; Q2KIU2; -.
DR   SMR; Q2KIU2; -.
DR   STRING; 9913.ENSBTAP00000023689; -.
DR   PaxDb; Q2KIU2; -.
DR   PeptideAtlas; Q2KIU2; -.
DR   PRIDE; Q2KIU2; -.
DR   GeneID; 513533; -.
DR   KEGG; bta:513533; -.
DR   CTD; 10654; -.
DR   eggNOG; ENOG502QYPQ; Eukaryota.
DR   InParanoid; Q2KIU2; -.
DR   OrthoDB; 1307762at2759; -.
DR   UniPathway; UPA00057; UER00099.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005919; Pmev_kin_anim.
DR   PANTHER; PTHR13101; PTHR13101; 1.
DR   Pfam; PF04275; P-mevalo_kinase; 1.
DR   PIRSF; PIRSF036639; PMK_anim; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01223; Pmev_kin_anim; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW   Kinase; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..192
FT                   /note="Phosphomevalonate kinase"
FT                   /id="PRO_0000239739"
FT   BINDING         17..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q15126"
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q15126"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q15126"
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q15126"
FT   BINDING         180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q15126"
SQ   SEQUENCE   192 AA;  21956 MW;  CE84F6A99EAEEF05 CRC64;
     MAPLGGVPGL VLLFSGKRKS GKDFVTEALQ SRLGADVCAI LRLSGPLKEQ YAQEHGLDFQ
     RLMDASTYKE AYRSDMIRWG EEKRQADPGF FCRKIVEGVC QPVWLVSDTR RVSDIQWFQE
     AYGAVTQTVR VVATEESRQQ RGWVFTPGVD DAESECGLDN FRTFDWVIEN HGDEQHLEEQ
     LEHLIEFIRS RL