ID A0A160VUU8_9EURY Unreviewed; 333 AA.
AC A0A160VUU8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=A3L04_04415 {ECO:0000313|EMBL:ASJ16369.1}, CHITON_1860
GN {ECO:0000313|EMBL:CUX78639.1};
OS Thermococcus chitonophagus.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=54262 {ECO:0000313|EMBL:CUX78639.1, ECO:0000313|Proteomes:UP000093069};
RN [1] {ECO:0000313|Proteomes:UP000093069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Vorgias C.E.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CUX78639.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1 {ECO:0000313|EMBL:CUX78639.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ASJ16369.1, ECO:0000313|Proteomes:UP000250189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GC74 {ECO:0000313|EMBL:ASJ16369.1,
RC ECO:0000313|Proteomes:UP000250189};
RA Oger P.M.;
RT "Complete genome sequence of Thermococcus chitonophagus type strain GC74.";
RL Submitted (APR-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; CP015193; ASJ16369.1; -; Genomic_DNA.
DR EMBL; LN999010; CUX78639.1; -; Genomic_DNA.
DR RefSeq; WP_068578833.1; NZ_LN999010.1.
DR AlphaFoldDB; A0A160VUU8; -.
DR STRING; 54262.CHITON_1860; -.
DR GeneID; 33321793; -.
DR KEGG; tch:CHITON_1860; -.
DR OrthoDB; 19001at2157; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000093069; Chromosome i.
DR Proteomes; UP000250189; 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; GHMP kinase, C-terminal domain; 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_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; 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00217};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00217};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00217}.
FT DOMAIN 102..168
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 242..310
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00217"
FT BINDING 109..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00217"
SQ SEQUENCE 333 AA; 35463 MW; 9E59F42010E04712 CRC64;
MRVLASAPAK IILFGEHSVV YGKPAIAAAI NLRTYVEAEL RDDKKIRIEA HDIKVPGLTV
SFSENEIYFE SDYGKAAEVL SYVRQAIELA MEEAGVRRGI NVSITSQIPV GAGLGSSAAV
AVATIGAVSK LLGLELTREE VAKLGHKVEL LVQGASSGID PTVSAIGGFL YYEKGNFEHL
PFMELPIVVG YTGSSGSTKE LVAMVRRRYE SMPELIVPIL NAMGKLVEKA REVITSELDE
EEKFAKLGEL MNINHGLLDA LGVSTKKLSE LVYAARTAGA LGAKITGAGG GGCMYALAPG
RQREVATAIT IAGGTPMITE ISREGLRIEE VMK
//
