ID   MVK_THEKO               Reviewed;         337 AA.
AC   Q5JJC6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Mevalonate kinase {ECO:0000255|HAMAP-Rule:MF_00217};
DE            Short=MK {ECO:0000255|HAMAP-Rule:MF_00217};
DE            Short=MVK {ECO:0000255|HAMAP-Rule:MF_00217};
DE            EC=2.7.1.36 {ECO:0000255|HAMAP-Rule:MF_00217};
GN   Name=mvk {ECO:0000255|HAMAP-Rule:MF_00217}; OrderedLocusNames=TK1474;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-
CC       mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA)
CC       pathway leading to isopentenyl diphosphate (IPP), a key precursor for
CC       the biosynthesis of isoprenoid compounds such as archaeal membrane
CC       lipids. {ECO:0000255|HAMAP-Rule:MF_00217}.
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:0000255|HAMAP-Rule:MF_00217};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00217};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 1/3. {ECO:0000255|HAMAP-Rule:MF_00217}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00217}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00217}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00217}.
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DR   EMBL; AP006878; BAD85663.1; -; Genomic_DNA.
DR   RefSeq; WP_011250425.1; NC_006624.1.
DR   AlphaFoldDB; Q5JJC6; -.
DR   SMR; Q5JJC6; -.
DR   STRING; 69014.TK1474; -.
DR   EnsemblBacteria; BAD85663; BAD85663; TK1474.
DR   GeneID; 3235187; -.
DR   KEGG; tko:TK1474; -.
DR   PATRIC; fig|69014.16.peg.1435; -.
DR   eggNOG; arCOG01028; Archaea.
DR   HOGENOM; CLU_017814_0_0_2; -.
DR   InParanoid; Q5JJC6; -.
DR   OMA; NTVCTYG; -.
DR   OrthoDB; 90882at2157; -.
DR   PhylomeDB; Q5JJC6; -.
DR   UniPathway; UPA00057; UER00098.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004496; F:mevalonate kinase activity; 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   HAMAP; MF_00217; Mevalonate_kinase; 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; IPR022937; Mevalonate_kinase_arc.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Isoprene biosynthesis; Kinase; Lipid biosynthesis;
KW   Lipid metabolism; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..337
FT                   /note="Mevalonate kinase"
FT                   /id="PRO_0000156670"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT   BINDING         113..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
SQ   SEQUENCE   337 AA;  35598 MW;  124D05A055E95A15 CRC64;
     MSVKRVLASA PAKIILFGEH SVVYGKPAIA AAIDLRTYVS AEFNDTGAIK IEAHDIRTPG
     LIVSFTEDSI YFESDYGKAA EVLGYVRQAI ELVREEADVN GKGITVSITS QIPVGAGLGS
     SAAVAVATIG AVSRLLGLEL SNEEVGKLGH KVELLVQGAS SGIDPTVSAI GGFIHYQKGK
     FEHLPFMELP LVVGYTGSSG STKELVAMVR KNYEEMPEIF EPILNSMGRL VEKAREVITS
     DLDRELKFQT LGKLMNINHG LLDALGVSTK KLSELVYAAR TAGALGAKIT GAGGGGCMYA
     LAPGKQSEVA TAITIAGGTP MITKISREGM RIEEVEE