ID   MVK_AERPE               Reviewed;         324 AA.
AC   Q9Y946;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=APE_2439;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA81454.1; -; Genomic_DNA.
DR   PIR; F72474; F72474.
DR   AlphaFoldDB; Q9Y946; -.
DR   SMR; Q9Y946; -.
DR   STRING; 272557.APE_2439; -.
DR   EnsemblBacteria; BAA81454; BAA81454; APE_2439.
DR   KEGG; ape:APE_2439; -.
DR   PATRIC; fig|272557.25.peg.1620; -.
DR   eggNOG; arCOG01028; Archaea.
DR   OMA; HSAVYGF; -.
DR   UniPathway; UPA00057; UER00098.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
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   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; 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.
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..324
FT                   /note="Mevalonate kinase"
FT                   /id="PRO_0000156663"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT   BINDING         103..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
SQ   SEQUENCE   324 AA;  33647 MW;  8D4FC2B63C11E846 CRC64;
     MRRAARASAP GKVIIVGEHF VVRGSLAIVA AIGRRLRVTV RSGGKGIVLE SSMLGRHSAP
     LPGQGAAAKV SPVLEPYIAV LRSLAARGYS VVPHTILVES GIPPRAGLGS SAASMVAYAL
     SYSAMHGDPL SAEDLYSVAM EGEKIAHGKP SGVDVTIAVR GGVLAYRRGE NPVDIRPGLT
     GVTLLVADTG VERRTRDVVE HVLSIADALG EASTYIYRAA DLIAREALHA IEKGDAERLG
     LIMNAAQGLL SSLGASSLEI ETLVYRMRSA GALGAKLTGA GWGGCVIGLF KEGEVERGLE
     SVVESSSQAF TASIAEEGAR LEEF