ID   ISPE_MYCTO              Reviewed;         318 AA.
AC   P9WKG6; L0T5K3; O05596; P65178;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
DE            Short=CMK {ECO:0000255|HAMAP-Rule:MF_00061};
DE            EC=2.7.1.148 {ECO:0000255|HAMAP-Rule:MF_00061};
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000255|HAMAP-Rule:MF_00061};
GN   Name=ispE {ECO:0000255|HAMAP-Rule:MF_00061}; OrderedLocusNames=MT1040;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC       of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000255|HAMAP-
CC       Rule:MF_00061}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00061};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 3/6. {ECO:0000255|HAMAP-Rule:MF_00061}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00061}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK45290.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WKG7};
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DR   EMBL; AE000516; AAK45290.1; ALT_INIT; Genomic_DNA.
DR   PIR; F70603; F70603.
DR   RefSeq; WP_003405199.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKG6; -.
DR   SMR; P9WKG6; -.
DR   EnsemblBacteria; AAK45290; AAK45290; MT1040.
DR   KEGG; mtc:MT1040; -.
DR   PATRIC; fig|83331.31.peg.1115; -.
DR   HOGENOM; CLU_053057_1_1_11; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000001020; 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   PIRSF; PIRSF010376; IspE; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00154; ispE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..318
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT                   /id="PRO_0000427657"
FT   ACT_SITE        25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   ACT_SITE        152
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   BINDING         110..120
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   318 AA;  32613 MW;  D3599C4B63EA3461 CRC64;
     MSASDGNTAE LWVPTGSVTV RVPGKVNLYL AVGDRREDGY HELTTVFHAV SLVDEVTVRN
     ADVLSLELVG EGADQLPTDE RNLAWQAAEL MAEHVGRAPD VSIMIDKSIP VAGGMAGGSA
     DAAAVLVAMN SLWELNVPRR DLRMLAARLG SDVPFALHGG TALGTGRGEE LATVLSRNTF
     HWVLAFADSG LLTSAVYNEL DRLREVGDPP RLGEPGPVLA ALAAGDPDQL APLLGNEMQA
     AAVSLDPALA RALRAGVEAG ALAGIVSGSG PTCAFLCTSA SSAIDVGAQL SGAGVCRTVR
     VATGPVPGAR VVSAPTEV