ID   ISPE_ECOLI              Reviewed;         283 AA.
AC   P62615; P24209;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase;
DE            Short=CMK;
DE            EC=2.7.1.148 {ECO:0000269|PubMed:10570138, ECO:0000269|PubMed:10655484, ECO:0000269|Ref.6};
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
GN   Name=ispE; Synonyms=ipk, ychB {ECO:0000303|PubMed:10570138};
GN   OrderedLocusNames=b1208, JW1199;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1427085; DOI=10.1016/0378-1119(92)90170-t;
RA   Ikemi M., Murakami K., Hashimoto M., Murooka Y.;
RT   "Cloning and characterization of genes involved in the biosynthesis of
RT   delta-aminolevulinic acid in Escherichia coli.";
RL   Gene 121:127-132(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7679718; DOI=10.1099/00221287-139-2-259;
RA   Post D.A., Hove-Jensen B., Switzer R.L.;
RT   "Characterization of the hemA-prs region of the Escherichia coli and
RT   Salmonella typhimurium chromosomes: identification of two open reading
RT   frames and implications for prs expression.";
RL   J. Gen. Microbiol. 139:259-266(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7543480; DOI=10.1128/jb.177.15.4488-4500.1995;
RA   Strohmaier H., Remler P., Renner W., Hoegenauer G.;
RT   "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic
RT   acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is
RT   growth phase regulated primarily at the transcriptional level in
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 177:4488-4500(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=10570138; DOI=10.1073/pnas.96.24.13714;
RA   Lange B.M., Croteau R.;
RT   "Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway:
RT   isopentenyl monophosphate kinase catalyzes the terminal enzymatic step.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13714-13719(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10655484; DOI=10.1073/pnas.97.3.1062;
RA   Luettgen H., Rohdich F., Herz S., Wungsintaweekul J., Hecht S.,
RA   Schuhr C.A., Fellermeier M., Sagner S., Zenk M.H., Bacher A.,
RA   Eisenreich W.;
RT   "Biosynthesis of terpenoids: YchB protein of Escherichia coli
RT   phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-D-
RT   erythritol.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:1062-1067(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Kuzuyama T., Takagi M., Kaneda K., Watanabe H., Dairi T., Seto H.;
RT   "Studies on the nonmevalonate pathway: conversion of 4-(cytidine 5'-
RT   diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-
RT   (cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase.";
RL   Tetrahedron Lett. 41:2925-2928(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [10]
RP   MUTAGENESIS OF GLY-239 AND THR-240.
RX   PubMed=12859972; DOI=10.1016/s0006-291x(03)01211-7;
RA   Sauret-Gueeto S., Ramos-Valdivia A., Ibanez E., Boronat A.,
RA   Rodriguez-Concepcion M.;
RT   "Identification of lethal mutations in Escherichia coli genes encoding
RT   enzymes of the methylerythritol phosphate pathway.";
RL   Biochem. Biophys. Res. Commun. 307:408-415(2003).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC       of 4-diphosphocytidyl-2C-methyl-D-erythritol (PubMed:10570138,
CC       PubMed:10655484, Ref.6). Phosphorylates isopentenyl phosphate at low
CC       rates. Also acts on isopentenol, and, much less efficiently,
CC       dimethylallyl alcohol. Dimethylallyl monophosphate does not serve as a
CC       substrate (PubMed:10570138). {ECO:0000269|PubMed:10570138,
CC       ECO:0000269|PubMed:10655484, ECO:0000269|Ref.6}.
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:0000269|PubMed:10570138, ECO:0000269|PubMed:10655484,
CC         ECO:0000269|Ref.6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18438;
CC         Evidence={ECO:0000269|PubMed:10570138, ECO:0000269|PubMed:10655484,
CC         ECO:0000269|Ref.6};
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:0000305|PubMed:10570138}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P62615; P17169: glmS; NbExp=2; IntAct=EBI-562202, EBI-551022;
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be an isopentenyl monophosphate
CC       kinase. {ECO:0000305|PubMed:1427085}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01106.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D10264; BAA01106.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; M77237; AAA24434.1; -; Genomic_DNA.
DR   EMBL; U18555; AAC43434.1; -; Genomic_DNA.
DR   EMBL; AJ249325; CAB64963.1; -; Genomic_DNA.
DR   EMBL; AF179284; AAF13867.1; -; Genomic_DNA.
DR   EMBL; AF216300; AAF29530.1; -; Genomic_DNA.
DR   EMBL; AB037116; BAA94247.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74292.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA36066.1; -; Genomic_DNA.
DR   PIR; B47706; B47706.
DR   RefSeq; NP_415726.1; NC_000913.3.
DR   RefSeq; WP_001260332.1; NZ_SSZK01000010.1.
DR   PDB; 2WW4; X-ray; 2.00 A; A/B=1-283.
DR   PDBsum; 2WW4; -.
DR   AlphaFoldDB; P62615; -.
DR   SMR; P62615; -.
DR   BioGRID; 4260815; 299.
DR   DIP; DIP-48028N; -.
DR   IntAct; P62615; 1.
DR   STRING; 511145.b1208; -.
DR   BindingDB; P62615; -.
DR   ChEMBL; CHEMBL2366480; -.
DR   jPOST; P62615; -.
DR   PaxDb; 511145-b1208; -.
DR   EnsemblBacteria; AAC74292; AAC74292; b1208.
DR   GeneID; 945774; -.
DR   KEGG; ecj:JW1199; -.
DR   KEGG; eco:b1208; -.
DR   PATRIC; fig|1411691.4.peg.1076; -.
DR   EchoBASE; EB1271; -.
DR   eggNOG; COG1947; Bacteria.
DR   HOGENOM; CLU_053057_3_0_6; -.
DR   InParanoid; P62615; -.
DR   OMA; RWPSPAK; -.
DR   OrthoDB; 9809438at2; -.
DR   PhylomeDB; P62615; -.
DR   BioCyc; EcoCyc:EG11294-MONOMER; -.
DR   BioCyc; MetaCyc:EG11294-MONOMER; -.
DR   BRENDA; 2.7.1.148; 2026.
DR   UniPathway; UPA00056; UER00094.
DR   PRO; PR:P62615; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
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; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Isoprene biosynthesis; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..283
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT                   /id="PRO_0000189215"
FT   ACT_SITE        10
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000250"
FT   BINDING         99..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         239
FT                   /note="G->R: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:12859972"
FT   MUTAGEN         240
FT                   /note="T->I: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:12859972"
FT   CONFLICT        208..276
FT                   /note="SNDCEVIARKRFREVDAVLSWLLEYAPSRLTGTGACVFAEFDTESEARQVLE
FT                   QAPEWLNGFVAKGANLS -> TQAYGRANTKGAPFRRTAVKCRSLGKLLLECAGKCLLR
FT                   VEAVLQRDVQNRTRSQA (in Ref. 1; BAA01106)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..20
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          26..49
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           66..80
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          89..95
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           106..121
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           142..147
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          151..154
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   TURN            155..158
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           181..185
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           199..203
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           212..218
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           220..230
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          244..250
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           251..260
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   STRAND          267..275
FT                   /evidence="ECO:0007829|PDB:2WW4"
FT   HELIX           277..281
FT                   /evidence="ECO:0007829|PDB:2WW4"
SQ   SEQUENCE   283 AA;  30925 MW;  59A2921FA05D13E1 CRC64;
     MRTQWPSPAK LNLFLYITGQ RADGYHTLQT LFQFLDYGDT ISIELRDDGD IRLLTPVEGV
     EHEDNLIVRA ARLLMKTAAD SGRLPTGSGA NISIDKRLPM GGGLGGGSSN AATVLVALNH
     LWQCGLSMDE LAEMGLTLGA DVPVFVRGHA AFAEGVGEIL TPVDPPEKWY LVAHPGVSIP
     TPVIFKDPEL PRNTPKRSIE TLLKCEFSND CEVIARKRFR EVDAVLSWLL EYAPSRLTGT
     GACVFAEFDT ESEARQVLEQ APEWLNGFVA KGANLSPLHR AML
//