MVK_PYRFU
ID MVK_PYRFU Reviewed; 334 AA.
AC Q8U0F3;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=PF1637;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(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; AE009950; AAL81761.1; -; Genomic_DNA.
DR RefSeq; WP_011012784.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0F3; -.
DR SMR; Q8U0F3; -.
DR STRING; 186497.PF1637; -.
DR EnsemblBacteria; AAL81761; AAL81761; PF1637.
DR GeneID; 41713462; -.
DR KEGG; pfu:PF1637; -.
DR PATRIC; fig|186497.12.peg.1703; -.
DR eggNOG; arCOG01028; Archaea.
DR HOGENOM; CLU_017814_0_0_2; -.
DR OMA; NTVCTYG; -.
DR OrthoDB; 90882at2157; -.
DR PhylomeDB; Q8U0F3; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000001013; 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..334
FT /note="Mevalonate kinase"
FT /id="PRO_0000156668"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
FT BINDING 110..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00217"
SQ SEQUENCE 334 AA; 35606 MW; B1ABB8A1994B5083 CRC64;
MKVIASAPAK VILFGEHSVV YGKPAIAAAI DLRTFVEAEL IREKKIRIEA HDIKVPGLTV
SFSENEIYFE TDYGKAAEVL SYVREAINLV LEEADKKNVG IKVSITSQIP VGAGLGSSAA
VAVATIGAVS KLLGLELSKE EIAKMGHKTE LLVQGASSGI DPTVSAIGGF IFYEKGKFEH
LPFMELPIVV GYTGSSGPTK ELVAMVRKRY EEMPELIVPI LEAMGKVVEK AKDVILSNVD
KEEKFERLGV LMNINHGLLD ALGVSTKKLS ELVYAARVAG ALGAKITGAG GGGCMYALAP
NKQREVATAI RIAGGTPMIT EISREGLKIE EVIK
