ID   PMK_SACS2               Reviewed;         323 AA.
AC   Q97UL6;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Phosphomevalonate kinase;
DE            Short=PMK;
DE            EC=2.7.4.2;
GN   OrderedLocusNames=SSO2988;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND PATHWAY.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
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 such as
CC       archaeal membrane lipids. {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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=77 uM for (R,S)-5-phosphomevalonate (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:23378249};
CC         Vmax=5.1 umol/min/mg enzyme (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:23378249};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 2/3. {ECO:0000269|PubMed:23378249}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
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DR   EMBL; AE006641; AAK43093.1; -; Genomic_DNA.
DR   PIR; F90479; F90479.
DR   RefSeq; WP_009992639.1; NC_002754.1.
DR   AlphaFoldDB; Q97UL6; -.
DR   SMR; Q97UL6; -.
DR   STRING; 273057.SSO2988; -.
DR   EnsemblBacteria; AAK43093; AAK43093; SSO2988.
DR   GeneID; 44128717; -.
DR   KEGG; sso:SSO2988; -.
DR   PATRIC; fig|273057.12.peg.3082; -.
DR   eggNOG; arCOG01032; Archaea.
DR   HOGENOM; CLU_076270_0_0_2; -.
DR   InParanoid; Q97UL6; -.
DR   OMA; KVLWIGS; -.
DR   PhylomeDB; Q97UL6; -.
DR   BRENDA; 2.7.4.2; 6163.
DR   SABIO-RK; Q97UL6; -.
DR   UniPathway; UPA00057; UER00099.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IBA:GO_Central.
DR   GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
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; 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.
PE   1: Evidence at protein level;
KW   ATP-binding; Isoprene biosynthesis; Kinase; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..323
FT                   /note="Phosphomevalonate kinase"
FT                   /id="PRO_0000429455"
SQ   SEQUENCE   323 AA;  36208 MW;  D62E48552F5CBDF8 CRC64;
     MIKVSAPGKI LWIGSYSVVF GGISHVIAVN KRVSCSLREI KEKDSLIFHT SYGHFKNSGN
     ELINSVLDTF RERLSQLPQG YEIDLYNDKE FIIDGKKTGL GSSSAATVSL TACLYYAIHG
     KLDLFEIHKL AQIANYKRQK GIGSGFDIAS AVFGSIVYKR FTDLDKMDFY FEKLNLGNYD
     MMLGFTGKSS ETVGLVRKFV EKSNLDDFKE IMRLIDEENY MAIKLIKLNK LDEAVEHIKL
     GRKYLNYIAE RIVGVKLVSK MEEELIKIAE EEGALVALSP GAGGGDSIFA LGNDLNRVRE
     AWSKRGIFII DVKEDEGLRL ESN