MVP5K_THEAC
ID MVP5K_THEAC Reviewed; 202 AA.
AC Q9HK44;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Mevalonate-3-phosphate 5-kinase {ECO:0000303|PubMed:24914732};
DE EC=2.7.1.186 {ECO:0000269|PubMed:24914732};
GN OrderedLocusNames=Ta0762 {ECO:0000312|EMBL:CAC11895.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=24914732; DOI=10.1021/bi500566q;
RA Vinokur J.M., Korman T.P., Cao Z., Bowie J.U.;
RT "Evidence of a novel mevalonate pathway in archaea.";
RL Biochemistry 53:4161-4168(2014).
RN [3]
RP PATHWAY.
RX PubMed=28004831; DOI=10.1038/srep39737;
RA Vinokur J.M., Cummins M.C., Korman T.P., Bowie J.U.;
RT "An adaptation to life in acid through a novel mevalonate pathway.";
RL Sci. Rep. 6:39737-39737(2016).
CC -!- FUNCTION: Phosphorylates mevalonate 3-phosphate to form mevalonate 3,5-
CC bisphosphate. Functions in an alternative mevalonate pathway, only
CC present in extreme acidophiles of the Thermoplasmatales order, which
CC passes through mevalonate 3-phosphate rather than mevalonate 5-
CC phosphate. {ECO:0000269|PubMed:24914732}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-phosphomevalonate + ATP = (R)-3,5-bisphosphomevalonate +
CC ADP + H(+); Xref=Rhea:RHEA:42888, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:82773, ChEBI:CHEBI:82774,
CC ChEBI:CHEBI:456216; EC=2.7.1.186;
CC Evidence={ECO:0000269|PubMed:24914732};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 9.0 sec(-1). {ECO:0000269|PubMed:24914732};
CC pH dependence:
CC Does not demonstrate significant pH dependence in the pH range of
CC 6.5-9.0. {ECO:0000269|PubMed:24914732};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:24914732};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway. {ECO:0000269|PubMed:24914732,
CC ECO:0000305|PubMed:28004831}.
CC -!- MISCELLANEOUS: It is proposed that Thermoplasmatales adapted the
CC classical archaeal mevalonate pathway by replacing mevalonate 5-
CC phosphate decarboxylase (MMD) with two specialized enzymes (mevalonate-
CC 3-phosphate 5-kinase and mevalonate 3,5-bisphosphate decarboxylase) in
CC order to produce isoprenoids in extremely acidic environments. It was
CC found that at low pH, the dual function enzyme MMD is unable to carry
CC out the first phosphorylation step, yet retains its ability to perform
CC decarboxylation. {ECO:0000305|PubMed:28004831}.
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DR EMBL; AL445065; CAC11895.1; -; Genomic_DNA.
DR RefSeq; WP_010901177.1; NC_002578.1.
DR AlphaFoldDB; Q9HK44; -.
DR STRING; 273075.Ta0762; -.
DR EnsemblBacteria; CAC11895; CAC11895; CAC11895.
DR GeneID; 1456320; -.
DR KEGG; tac:Ta0762; -.
DR eggNOG; arCOG01967; Archaea.
DR HOGENOM; CLU_1412410_0_0_2; -.
DR OMA; DRINYTH; -.
DR OrthoDB; 106753at2157; -.
DR BioCyc; MetaCyc:MON-18736; -.
DR BRENDA; 2.7.1.186; 6324.
DR UniPathway; UPA00057; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Isoprene biosynthesis; Kinase; Lipid biosynthesis;
KW Lipid metabolism; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..202
FT /note="Mevalonate-3-phosphate 5-kinase"
FT /id="PRO_0000431279"
SQ SEQUENCE 202 AA; 23298 MW; BEFC02FB73FC612C CRC64;
MNSRIMFIGG VPGVGKTSIS GYIARNTDID IVLSSDYLRE FLRPFAPQES HLETSVYDAW
KFYGDMSDDN IIRGYLDQAR PIMGGINRVI ARALANGEDL IIESLYFVPD MMDEMVLKNA
FLAYVYIDDP DLHRSRLEDR INYTHRNSPG SRLAAHLKEY RTIMDYSMDM ARGRGIGLYS
TDDYALARQR LLDDFRKFVD RR
