MVK_THESM
ID MVK_THESM Reviewed; 333 AA.
AC C6A3T5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=TSIB_1226;
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739;
RX PubMed=19447963; DOI=10.1128/aem.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
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; CP001463; ACS90280.1; -; Genomic_DNA.
DR RefSeq; WP_015849499.1; NC_012883.1.
DR AlphaFoldDB; C6A3T5; -.
DR SMR; C6A3T5; -.
DR STRING; 604354.TSIB_1226; -.
DR EnsemblBacteria; ACS90280; ACS90280; TSIB_1226.
DR GeneID; 8096224; -.
DR KEGG; tsi:TSIB_1226; -.
DR eggNOG; arCOG01028; Archaea.
DR HOGENOM; CLU_017814_0_0_2; -.
DR OMA; NTVCTYG; -.
DR OrthoDB; 90882at2157; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000009079; 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; 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..333
FT /note="Mevalonate kinase"
FT /id="PRO_1000204228"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT BINDING 109..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
SQ SEQUENCE 333 AA; 35408 MW; 5D70B6352D620BB1 CRC64;
MRVLASAPAK IILFGEHSVV YGKPAIAAAI DLRTYVKAEF NENGRIRIEA KDIRTPGLTV
SFSEDQIYFE TDYGKAAEVL SYVREAINLV MEEAEKQKGV TVSITSQIPV GAGLGSSAAV
AVATIGAVSR LFGLELTPEE VAKLGHKVEL LVQGASSGID PTVSAIGGFL YYQKGSFESL
PVVELPIVVG YTGSSGSTKE LVAKVRKNYE EMPEIIDPIL NSMGRLVEKA REVILAEYDK
EIKFKRLGTL MNINHGLLDA LGVSTKSLSD LVYASREAGA LGAKITGAGG GGCMYALAPE
KQSEVATAIK IAGGMPIVTK ISREGLRIED IVQ
