ID A0A2I0PB68_9EURY Unreviewed; 289 AA.
AC A0A2I0PB68;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Mevalonate kinase {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|HAMAP-Rule:MF_00217};
GN Name=mvk {ECO:0000256|HAMAP-Rule:MF_00217,
GN ECO:0000313|EMBL:PKL63484.1};
GN ORFNames=CVV31_00070 {ECO:0000313|EMBL:PKL63484.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-2.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013818 {ECO:0000313|EMBL:PKL63484.1, ECO:0000313|Proteomes:UP000233573};
RN [1] {ECO:0000313|EMBL:PKL63484.1, ECO:0000313|Proteomes:UP000233573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-2 {ECO:0000313|EMBL:PKL63484.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
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|HAMAP-Rule:MF_00217}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKL63484.1}.
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DR EMBL; PGYL01000001; PKL63484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0PB68; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000233573; 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: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; -; 2.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR HAMAP; MF_00217; Mevalonate_kinase; 1.
DR InterPro; IPR001174; Galkinase.
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_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; PR00960; LMBPPROTEIN.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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|HAMAP-Rule:MF_00217, ECO:0000313|EMBL:PKL63484.1};
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}; Transferase {ECO:0000256|HAMAP-Rule:MF_00217}.
FT DOMAIN 64..131
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 193..266
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00217"
SQ SEQUENCE 289 AA; 30397 MW; A86196135F3EF0AF CRC64;
MATWSAPGKI FLFGEHAVVY GKPGVAMAIK PRVFVTVRKS RNPTRAKSPY IDECFKLMGV
RGSVYVHSQL QSSSGLGSSA AVTVATLSAI NDEFGLGRTR EFIADAAFSV EKKVQKGRAS
PTDTYVSANG GMVLITGNSK RRLPPEGLQV VVGNTLVPHS TARMVEQVGD LQRRHPDVAN
PILDAIGAVT LAALHNINNP KELGQYMDMN HALLEALGVG HPTSSKLVLA ARASGAYGAK
ITGAGGGGCI IALCPRRAKS RVAGAIEACE GKAIITTIDT DGARKEKHD
//
