ID   ISPE_TROWT              Reviewed;         409 AA.
AC   Q83FU3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 93.
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=TWT_605;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO44702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014184; AAO44702.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_038104236.1; NC_004572.3.
DR   AlphaFoldDB; Q83FU3; -.
DR   SMR; Q83FU3; -.
DR   STRING; 203267.TWT_605; -.
DR   EnsemblBacteria; AAO44702; AAO44702; TWT_605.
DR   KEGG; twh:TWT_605; -.
DR   eggNOG; COG1947; Bacteria.
DR   HOGENOM; CLU_585165_0_0_11; -.
DR   OMA; LQNTHIL; -.
DR   OrthoDB; 1938933at2; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000002200; Chromosome.
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   Reference proteome; Transferase.
FT   CHAIN           1..409
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT                   /id="PRO_0000189284"
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;  43957 MW;  BEABB08A880ECC7D CRC64;
     MKTDGGNTWR ASHSKPLNTA NTMGEPFSHS EYSVHADQSE FYLNELTEHS GQDNPCMNTS
     RLNTNRYGHP VVHPCPKIHC ICTQSNIAAI GSDCTGCVDI AQACKMLRGG LGCTQDPCVK
     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