ID   MVK_PYRHO               Reviewed;         335 AA.
AC   O59291;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 136.
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=PH1625;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; Evidence={ECO:0000255|HAMAP-
CC         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; BA000001; BAA30737.1; -; Genomic_DNA.
DR   PIR; A71042; A71042.
DR   RefSeq; WP_010885698.1; NC_000961.1.
DR   AlphaFoldDB; O59291; -.
DR   SMR; O59291; -.
DR   STRING; 70601.gene:9378615; -.
DR   EnsemblBacteria; BAA30737; BAA30737; BAA30737.
DR   GeneID; 1442477; -.
DR   KEGG; pho:PH1625; -.
DR   eggNOG; arCOG01028; Archaea.
DR   OrthoDB; 19001at2157; -.
DR   UniPathway; UPA00057; UER00098.
DR   Proteomes; UP000000752; 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; GHMP kinase, C-terminal domain; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00549; mevalon_kin; 1.
DR   PANTHER; PTHR43290; MEVALONATE KINASE; 1.
DR   PANTHER; PTHR43290:SF2; MEVALONATE KINASE; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PRINTS; PR00959; MEVGALKINASE.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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; Transferase.
FT   CHAIN           1..335
FT                   /note="Mevalonate kinase"
FT                   /id="PRO_0000156669"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT   BINDING         111..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
SQ   SEQUENCE   335 AA;  35686 MW;  17D0A9E1D22A1EB1 CRC64;
     MVKYVLASAP AKVILFGEHS VVYGKPAIAS AIELRTYVRA QFNDSGNIKI EAHDIKTPGL
     IVSFSEDKIY FETDYGKAAE VLSYVRYAIE LALEESDKRV GIDVSITSQI PVGAGLGSSA
     AVAVATIGAV SRLLGLELSK EEIAKLGHKV ELLVQGASSG IDPTVSAVGG FLYYKQGKFE
     PLPFMELPIV VGYTGSTGST KELVAMVRKR YEEMPELVEP ILEAMGKLVD KAKEIILSKL
     DEEEKLTKLG ELMNINHGLL DALGVSTKKL GELVYAARTA GAIGAKLTGA GGGGCMYALA
     PGRQREVATA IKIAGGIPMI TRVSREGLRI EEVSR
//