MVK_SACS2
ID MVK_SACS2 Reviewed; 314 AA.
AC Q980D2;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=SSO0383;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=23378249; DOI=10.1093/jb/mvt006;
RA Nishimura H., Azami Y., Miyagawa M., Hashimoto C., Yoshimura T., Hemmi H.;
RT "Biochemical evidence supporting the presence of the classical mevalonate
RT pathway in the thermoacidophilic archaeon Sulfolobus solfataricus.";
RL J. Biochem. 153:415-420(2013).
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, ECO:0000269|PubMed:23378249}.
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 ECO:0000269|PubMed:23378249};
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 ECO:0000269|PubMed:23378249}.
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; AE006641; AAK40711.1; -; Genomic_DNA.
DR PIR; H90181; H90181.
DR RefSeq; WP_010922957.1; NC_002754.1.
DR AlphaFoldDB; Q980D2; -.
DR SMR; Q980D2; -.
DR STRING; 273057.SSO0383; -.
DR EnsemblBacteria; AAK40711; AAK40711; SSO0383.
DR GeneID; 44129357; -.
DR KEGG; sso:SSO0383; -.
DR PATRIC; fig|273057.12.peg.377; -.
DR eggNOG; arCOG01028; Archaea.
DR HOGENOM; CLU_017814_0_0_2; -.
DR InParanoid; Q980D2; -.
DR OMA; NTVCTYG; -.
DR PhylomeDB; Q980D2; -.
DR BRENDA; 2.7.1.36; 6163.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000001974; 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; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Isoprene biosynthesis; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..314
FT /note="Mevalonate kinase"
FT /id="PRO_0000429457"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT BINDING 103..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
SQ SEQUENCE 314 AA; 34542 MW; B2E968C32ED15117 CRC64;
MMVEAKVPLK LTLFGEHAVV YDRPAIAMTI SESLKVKVSE NDKFLIISPS LNIKGVKLDL
NEMKIESDEA KKVLRYVFEV LNYFEMKKPV KIEINSTVEP SVGLGTSAAV IVGTVAAYSK
YLGIDLSRDE IAKISHNIEL KVQGIASRMD TYTETYGGLI YFPAGGKGFE KIDTNFELTA
GYIRRSMSTA DVLWRVRTLK ESNKEVFENI LDVIGEITNR AKSLIVEQNF EELGLLMYVN
HGLLFSLGIT SPEADEIVSR AKQLGIKGCK ISGGGAGGSI ICIKSVEAEV LLRSYNARIV
NSTLTKDGVI FSIL
