ID A0A1I2RB59_9EURY Unreviewed; 338 AA.
AC A0A1I2RB59;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Mevalonate kinase {ECO:0000256|ARBA:ARBA00012103, ECO:0000256|HAMAP-Rule:MF_00217};
DE Short=MK {ECO:0000256|HAMAP-Rule:MF_00217};
DE Short=MVK {ECO:0000256|HAMAP-Rule:MF_00217};
DE EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103, ECO:0000256|HAMAP-Rule:MF_00217};
GN Name=mvk {ECO:0000256|HAMAP-Rule:MF_00217};
GN ORFNames=SAMN04488063_1855 {ECO:0000313|EMBL:SFG37700.1};
OS Halopelagius inordinatus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=553467 {ECO:0000313|EMBL:SFG37700.1, ECO:0000313|Proteomes:UP000198876};
RN [1] {ECO:0000313|Proteomes:UP000198876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7739 {ECO:0000313|Proteomes:UP000198876};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_00217};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|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:0000256|ARBA:ARBA00029438, ECO:0000256|HAMAP-
CC Rule:MF_00217}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00217}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00217}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00006495, ECO:0000256|HAMAP-
CC Rule:MF_00217}.
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DR EMBL; FOOQ01000002; SFG37700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2RB59; -.
DR STRING; 553467.SAMN04488063_1855; -.
DR OrthoDB; 19001at2157; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000198876; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004335; F:galactokinase activity; IEA:InterPro.
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:0006012; P:galactose metabolic process; IEA:InterPro.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR HAMAP; MF_00217; Mevalonate_kinase; 1.
DR InterPro; IPR000705; Galactokinase.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00549; mevalon_kin; 1.
DR PANTHER; PTHR43290; MEVALONATE KINASE; 1.
DR PANTHER; PTHR43290:SF2; MEVALONATE KINASE; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PRINTS; PR00473; GALCTOKINASE.
DR PRINTS; PR00959; MEVGALKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00217};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00217};
KW Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00217};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00217};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00217};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00217}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00217};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00217}; Reference proteome {ECO:0000313|Proteomes:UP000198876};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00217}.
FT DOMAIN 104..172
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 251..310
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00217"
FT BINDING 112..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00217"
SQ SEQUENCE 338 AA; 35437 MW; 191A24408B326890 CRC64;
MTVSSAPGKV YLFGEHAVVY GEPAVPCAVE RRAAVTVEAR DDDRIRVEAS DLSLDGFTVE
YGGTADRRPD VDVPASLLDA ATGYIDAAVE QARDAADAPD AGFDVTIESD IPLGAGLGSS
AAVVVAGIDA ATRELGVELE KTELADRAYR AEYEVQDGEA SRADTFCSTM GGAVRIEGDD
CRRIDTPNLP FVVGFDGGAG DTGELVAGVR ALREEYGFAA DTVENIGDIV RRGETLLSAA
DPGADPTEDL LTELGRLMNF DHGLLEALGV SSRTLDNMVW AAREAGAHGA KLTGAGGGGC
IVALDDTRET ETALRYTAEC ENAFRAELDR EGVRVEEA
//
