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Database: UniProt
Entry: A0A1F5ZTP4_9BACT
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ID   A0A1F5ZTP4_9BACT        Unreviewed;       319 AA.
AC   A0A1F5ZTP4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=mevalonate kinase {ECO:0000256|ARBA:ARBA00012103};
DE            EC=2.7.1.36 {ECO:0000256|ARBA:ARBA00012103};
GN   ORFNames=A3D77_01605 {ECO:0000313|EMBL:OGG15704.1};
OS   Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_02_FULL_39_11.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1798382 {ECO:0000313|EMBL:OGG15704.1, ECO:0000313|Proteomes:UP000176923};
RN   [1] {ECO:0000313|EMBL:OGG15704.1, ECO:0000313|Proteomes:UP000176923}
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:OGG15704.1}.
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DR   EMBL; MFJL01000019; OGG15704.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F5ZTP4; -.
DR   STRING; 1798382.A3D77_01605; -.
DR   UniPathway; UPA00057; UER00098.
DR   Proteomes; UP000176923; 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:OGG15704.1};
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          82..149
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
SQ   SEQUENCE   319 AA;  35297 MW;  D83B02CE3C746055 CRC64;
     MQITVSAPGK IHLLGEHAVV YGYPSLLSTI DKRLEVILTL LDKSNDTKEK IQIQTPEGTG
     LIYKSLEIFQ KAARLSQLPP LHIKVESDIP VGSGLGSSAA LSVALMGALF KGIKNLWNPV
     KINELAYEVE KLQHGNPSGG DNTVVTFGGL VWFRRETEFL KSIWNLPSAS YHLPSLILID
     SGRPKETTGE MVSYVNRLYT QKKTFYENIF KDQERETRNL LSALKKGDRE NVKRAFYRGE
     KNLEKMGVVG KKAQSLIRSI EKLGGFAKIS GAGGITEGSG MILCYLSNFE KIEEIAKKFG
     CNIHKVNLGV EGVRIENGE
//
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