ID A0A1F5JV30_9BACT Unreviewed; 313 AA.
AC A0A1F5JV30;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=mevalonate kinase {ECO:0000256|ARBA:ARBA00012103};
DE EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103};
GN ORFNames=A3C59_01445 {ECO:0000313|EMBL:OGE32516.1};
OS Candidatus Daviesbacteria bacterium RIFCSPHIGHO2_02_FULL_36_13.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1797768 {ECO:0000313|EMBL:OGE32516.1, ECO:0000313|Proteomes:UP000176902};
RN [1] {ECO:0000313|EMBL:OGE32516.1, ECO:0000313|Proteomes:UP000176902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3. {ECO:0000256|ARBA:ARBA00029438}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00006495}.
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:OGE32516.1}.
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DR EMBL; MFCV01000025; OGE32516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5JV30; -.
DR STRING; 1797768.A3C59_01445; -.
DR UniPathway; UPA00057; UER00098.
DR Proteomes; UP000176902; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004496; F:mevalonate kinase activity; IEA:UniProtKB-EC.
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 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; 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; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OGE32516.1};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 77..143
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
SQ SEQUENCE 313 AA; 34465 MW; FE45FEF3FA4278FC CRC64;
MKSGRNITVS APAKINLLGE HANVYGKPTI LTAIDLRATV TISQGRTIQK DFVFLQKIIE
KIIKKELKLK KIPLYSLNLS SKIPMGCGLG SSASLSAAYI GALLSYLRVK WDVNLINRLT
FEAEKVFHGN PSGSDNSSVV FGGLIWFRKE SPDLKLIHPL SFSIPSKLSR SFVLINTGKP
SESTKDMVAL VKNLYDKNPK LVDKVLEEQE KLVKELIPVL KKVNQKEFIR IIRKGEKNLE
SIGVVGKKAK KIIRKIESLG GTAKISGAGG VIADSGIILC FHKSKKVVIN IAKVYNLPYF
SVKLGVEGVR IEK
//
