ID   PMK_STRC1               Reviewed;         374 AA.
AC   Q9KWG3;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Phosphomevalonate kinase;
DE            Short=PMK;
DE            EC=2.7.4.2;
OS   Streptomyces sp. (strain CL190).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=93372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=CL190;
RX   PubMed=10894721; DOI=10.1128/jb.182.15.4153-4157.2000;
RA   Takagi M., Kuzuyama T., Takahashi S., Seto H.;
RT   "A gene cluster for the mevalonate pathway from Streptomyces sp. strain
RT   CL190.";
RL   J. Bacteriol. 182:4153-4157(2000).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=CL190;
RX   PubMed=23378249; DOI=10.1093/jb/mvt006;
RA   Nishimura H., Azami Y., Miyagawa M., Hashimoto C., Yoshimura T., Hemmi H.;
RT   "Biochemical evidence supporting the presence of the classical mevalonate
RT   pathway in the thermoacidophilic archaeon Sulfolobus solfataricus.";
RL   J. Biochem. 153:415-420(2013).
CC   -!- FUNCTION: Catalyzes the phosphorylation of (R)-mevalonate 5-phosphate
CC       (MVAP) to (R)-mevalonate 5-diphosphate (MVAPP). Functions in the
CC       mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a
CC       key precursor for the biosynthesis of isoprenoid compounds.
CC       {ECO:0000269|PubMed:23378249}.
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:23378249};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 2/3. {ECO:0000269|PubMed:10894721}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
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DR   EMBL; AB037666; BAB07792.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KWG3; -.
DR   SMR; Q9KWG3; -.
DR   UniPathway; UPA00057; UER00099.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:UniProtKB-EC.
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; 3.30.230.10; -; 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; IPR035102; Phosphomevalonate_kinase.
DR   InterPro; IPR005917; Pmev_kinase_bact.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR31814; PTHR31814; 3.
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; TIGR01220; Pmev_kin_Gr_pos; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Isoprene biosynthesis; Kinase; Magnesium; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..374
FT                   /note="Phosphomevalonate kinase"
FT                   /id="PRO_0000429456"
SQ   SEQUENCE   374 AA;  39281 MW;  A2908B333C694E6D CRC64;
     MTTGQRTIVR HAPGKLFVAG EYAVVDPGNP AILVAVDRHI SVTVSDADAD TGAADVVISS
     DLGPQAVGWR WHDGRLVVRD PDDGQQARSA LAHVVSAIET VGRLLGERGQ KVPALTLSVS
     SRLHEDGRKF GLGSSGAVTV ATVAAVAAFC GLELSTDERF RLAMLATAEL DPKGSGGDLA
     ASTWGGWIAY QAPDRAFVLD LARRVGVDRT LKAPWPGHSV RRLPAPKGLT LEVGWTGEPA
     STASLVSDLH RRTWRGSASH QRFVETTTDC VRSAVTALES GDDTSLLHEI RRARQELARL
     DDEVGLGIFT PKLTALCDAA EAVGGAAKPS GAGGGDCGIA LLDAEASRDI THVRQRWETA
     GVLPLPLTPA LEGI