ISPE_ECOL6
ID ISPE_ECOL6 Reviewed; 283 AA.
AC Q8FI04;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=c1666;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS), AND SUBUNIT.
RX PubMed=12878729; DOI=10.1073/pnas.1533425100;
RA Miallau L., Alphey M.S., Kemp L.E., Leonard G.A., McSweeney S.M., Hecht S.,
RA Bacher A., Eisenreich W., Rohdich F., Hunter W.N.;
RT "Biosynthesis of isoprenoids: crystal structure of 4-diphosphocytidyl-2C-
RT methyl-D-erythritol kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9173-9178(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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12878729}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN80131.1; -; Genomic_DNA.
DR RefSeq; WP_001260345.1; NC_004431.1.
DR PDB; 1OJ4; X-ray; 2.01 A; A/B=1-283.
DR PDBsum; 1OJ4; -.
DR AlphaFoldDB; Q8FI04; -.
DR SMR; Q8FI04; -.
DR STRING; 199310.c1666; -.
DR EnsemblBacteria; AAN80131; AAN80131; c1666.
DR KEGG; ecc:c1666; -.
DR eggNOG; COG1947; Bacteria.
DR HOGENOM; CLU_053057_3_0_6; -.
DR OMA; RWPSPAK; -.
DR BioCyc; ECOL199310:C1666-MON; -.
DR UniPathway; UPA00056; UER00094.
DR EvolutionaryTrace; Q8FI04; -.
DR Proteomes; UP000001410; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..283
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase"
FT /id="PRO_0000189217"
FT ACT_SITE 10
FT /evidence="ECO:0000305"
FT ACT_SITE 141
FT /evidence="ECO:0000305"
FT BINDING 99..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 2..20
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 26..49
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1OJ4"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:1OJ4"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1OJ4"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:1OJ4"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:1OJ4"
SQ SEQUENCE 283 AA; 30973 MW; E0327295E65EDDFC CRC64;
MRTQWPSPAK LNLFLYITGQ RADGYHTLQT LFQFLDYGDT ISIELRDDGD IRLLTPVEGV
EHEDNLIVRA ARLLMKTAAD SGRLSTGSGA NISIDKRLPM GGGLGGGSSN AATVLVALNH
LWQCGLSMDE LAEMGLTLGA DVPVFVRGHA AFAEGVGEIL MPVDPPEKWY LVAHPGVSIP
TPVIFKDPEL PRNTPKRSIE TLLKCEFSND CEVIARKRFR EVDAVLSWLL EYAPSRLTGT
GACVFAEFDT ESEARQVLEQ APEWLNGFVA KGVNLSPLHR AML
