MVK_ARCFU
ID MVK_ARCFU Reviewed; 284 AA.
AC O27995;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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=AF_2289;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB88965.1; -; Genomic_DNA.
DR PIR; A69536; A69536.
DR RefSeq; WP_010879778.1; NC_000917.1.
DR AlphaFoldDB; O27995; -.
DR SMR; O27995; -.
DR STRING; 224325.AF_2289; -.
DR EnsemblBacteria; AAB88965; AAB88965; AF_2289.
DR GeneID; 1485521; -.
DR KEGG; afu:AF_2289; -.
DR eggNOG; arCOG01028; Archaea.
DR HOGENOM; CLU_017814_0_0_2; -.
DR OMA; NTVCTYG; -.
DR OrthoDB; 90882at2157; -.
DR PhylomeDB; O27995; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000002199; 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; 2.
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..284
FT /note="Mevalonate kinase"
FT /id="PRO_0000156664"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT BINDING 86..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
SQ SEQUENCE 284 AA; 30877 MW; F102C1C71772CA7F CRC64;
MIASAPGKII LFGEHAVVYG RHAVVSAINL RCRVSVRKSD RFLIRSSLGE SGLDYQRHPY
VVQAVKRFGE LRNIPGAEIE IESEIPIGSG LGSSAAVIVA TIAALNAEFD GDMDKEAIFQ
MAKQVEIDVQ GRASGIDPFI STFGGSWLFP ERRKVEMPFK FFVINFGSRS TAEMVAKVAE
LRERHPEVVD KIFDAIDAIS LEASDVGSAE RLEELIAINQ SLLRAIGVSN PEIDRTIAEL
ERMGLNAKIT GAGGGGCIFG LFKGEKPKGS FIVEPEKEGV RIEE
