PMVK_PIG
ID PMVK_PIG Reviewed; 192 AA.
AC Q29081; F1RGP9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 4.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphomevalonate kinase;
DE Short=PMKase;
DE EC=2.7.4.2 {ECO:0000269|PubMed:6248100};
GN Name=PMVK;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-121.
RC TISSUE=Liver;
RX PubMed=8663599; DOI=10.1074/jbc.271.29.17330;
RA Chambliss K.L., Slaughter C.A., Schreiner R., Hoffmann G.F., Gibson K.M.;
RT "Molecular cloning of human phosphomevalonate kinase and identification of
RT a consensus peroxisomal targeting sequence.";
RL J. Biol. Chem. 271:17330-17334(1996).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=7814412; DOI=10.1074/jbc.270.1.461;
RA Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A.,
RA Jakobs C., Gibson K.M.;
RT "Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde
RT dehydrogenase from rat and human. cDNA isolation, evolutionary homology,
RT and tissue expression.";
RL J. Biol. Chem. 270:461-467(1995).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=6248100; DOI=10.1021/bi00552a003;
RA Bazaes S., Beytia E., Jabalquinto A.M., Solis de Ovando F., Gomez I.,
RA Eyzaguirre J.;
RT "Pig liver phosphomevalone kinase. 1. Purification and properties.";
RL Biochemistry 19:2300-2304(1980).
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:0000269|PubMed:6248100}.
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:0000269|PubMed:6248100};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC Evidence={ECO:0000305|PubMed:6248100};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16343;
CC Evidence={ECO:0000250|UniProtKB:Q15126};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.075 mM for phosphomevalonate {ECO:0000269|PubMed:6248100};
CC KM=0.46 mM for ATP {ECO:0000269|PubMed:6248100};
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:0000269|PubMed:6248100}.
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; CU207227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L77214; AAC37331.1; -; mRNA.
DR RefSeq; NP_001161888.1; NM_001168416.1.
DR AlphaFoldDB; Q29081; -.
DR SMR; Q29081; -.
DR STRING; 9823.ENSSSCP00000006964; -.
DR PaxDb; Q29081; -.
DR PeptideAtlas; Q29081; -.
DR PRIDE; Q29081; -.
DR Ensembl; ENSSSCT00000007157; ENSSSCP00000006964; ENSSSCG00000006535.
DR Ensembl; ENSSSCT00025039977; ENSSSCP00025016998; ENSSSCG00025029408.
DR Ensembl; ENSSSCT00035110593; ENSSSCP00035048279; ENSSSCG00035080644.
DR Ensembl; ENSSSCT00040102979; ENSSSCP00040046582; ENSSSCG00040074485.
DR Ensembl; ENSSSCT00045026000; ENSSSCP00045017945; ENSSSCG00045015312.
DR Ensembl; ENSSSCT00050027646; ENSSSCP00050011423; ENSSSCG00050020471.
DR Ensembl; ENSSSCT00055021592; ENSSSCP00055017104; ENSSSCG00055010989.
DR Ensembl; ENSSSCT00070056028; ENSSSCP00070047606; ENSSSCG00070027918.
DR GeneID; 100152301; -.
DR KEGG; ssc:100152301; -.
DR CTD; 10654; -.
DR VGNC; VGNC:98835; PMVK.
DR eggNOG; ENOG502QYPQ; Eukaryota.
DR GeneTree; ENSGT00390000014801; -.
DR InParanoid; Q29081; -.
DR OMA; YGFFCRA; -.
DR OrthoDB; 1307762at2759; -.
DR TreeFam; TF312935; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000006535; Expressed in liver and 47 other tissues.
DR Genevisible; F1RGP9; SS.
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; ISS:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
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 1: Evidence at protein level;
KW ATP-binding; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW Direct protein sequencing; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Nucleotide-binding; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..192
FT /note="Phosphomevalonate kinase"
FT /id="PRO_0000058474"
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"
FT CONFLICT 20
FT /note="S -> D (in Ref. 2; AAC37331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21943 MW; 9BEB4CD8FA1FBE38 CRC64;
MAPLGSVPRL VLLFSGKRKS GKDFVTEALQ SRLGADVCAI LRLSGPLKEQ YAQEHGLDFQ
RLLDASTYKE SYRKDMIRWG QEKRQADPGF FCRKIVEGVS QPIWLVSDTR RLSDIQWFQE
TYGAVTQTVR VVATEQSRQQ RGWVFIPGVD DAESECGLDD FGAFDWVIEN HGDEQHLEEQ
LGHLIEFVHS RL
