ID   ISPE_TROW8              Reviewed;         409 AA.
AC   Q83IA0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase;
DE            Short=CMK;
DE            EC=2.7.1.148;
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
GN   Name=ispE; OrderedLocusNames=TW159;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC       of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC         erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC         ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 3/6.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Cys-97 is present instead of the conserved Lys which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; BX251410; CAD66839.1; -; Genomic_DNA.
DR   RefSeq; WP_011096120.1; NC_004551.1.
DR   AlphaFoldDB; Q83IA0; -.
DR   SMR; Q83IA0; -.
DR   GeneID; 67387935; -.
DR   KEGG; tws:TW159; -.
DR   HOGENOM; CLU_585165_0_0_11; -.
DR   OMA; LQNTHIL; -.
DR   UniPathway; UPA00056; UER00094.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00061; IspE; 1.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR004424; IspE.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..409
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT                   /id="PRO_0000189283"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000250"
FT   BINDING         201..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   409 AA;  43972 MW;  25CF9B1DA0AADE71 CRC64;
     MKTDGGNTWR ASHSKPLNTA NTMGEPFSHS EYSVHADQSE FYLNELTEHS GQDNPCMNTS
     RLNTNRYGHP VVHPCPKIHC ICTQSNIAAI GSDCTGCVDI AQACKMLRGG QGCTQDPCVK
     NPHTQCFTDV SNHAMRNVLP LNVSNTEQFP IQIEYANGRN PVLNPMDDLA MRAALLLSKD
     IDLQNTHILP STRISIEKNI PVAAGLAGGS ADAAAVLLGI NSAWQTNYSR CDLLGKAGAL
     GADVPFLIWG GAAYGSGTGS CVTFFETQTL YWVLCFSKHP LSTRKVFQEL DRQRSGAGCN
     HHPVFSNPAE CAEMLKKAIK RGPEALAALL HNDLTSAAKM LMPEIAERIK AAERCPGILR
     AIISGSGPTL ALLAEDAEAA NRACSILKDT GVICKAVSSP AYSSIYWQT