ID   ISPE_THET2              Reviewed;         275 AA.
AC   Q72GN2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 108.
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};
GN   OrderedLocusNames=TT_C1816;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
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}.
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DR   EMBL; AE017221; AAS82158.1; -; Genomic_DNA.
DR   RefSeq; WP_011174171.1; NC_005835.1.
DR   AlphaFoldDB; Q72GN2; -.
DR   SMR; Q72GN2; -.
DR   GeneID; 3169608; -.
DR   KEGG; tth:TT_C1816; -.
DR   eggNOG; COG1947; Bacteria.
DR   HOGENOM; CLU_053057_1_1_0; -.
DR   OMA; AACLEMS; -.
DR   OrthoDB; 9809438at2; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000000592; 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 phosphate pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00154; ispE; 1.
DR   PANTHER; PTHR43527; 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43527:SF2; 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF010376; IspE; 1.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..275
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT                   /id="PRO_0000189278"
FT   ACT_SITE        8
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
FT   BINDING         86..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   275 AA;  29253 MW;  FBD398F091167202 CRC64;
     MERLAPAKVN LGLSVRFRRE DGYHELHTLF APFSLADRLV VEPVSSGLHF QGPYGRENLA
     YRAASLYLEA AGQPGGVRIL LEKRIPEGAG LGGGSSDAAQ VLLALQALYP AEVDLFALAR
     TLGADVPFFL LGRGAEARGV GERLKPLALP PVPAVVFFPG LRVPTPLVYR AVRPEDFGPD
     LPVEAILEAL ARGEEPPYWN SLEGPAFRLF PELKEVRGRM RALGLRGVLM SGSGSAFFGL
     AEGPDHARRA AEALRAWGRA WAGTLGGGDA GSGPA
//