(data stored in ACNUC10821 zone)

SWISSPROT: ISPE_LISMF

ID   ISPE_LISMF              Reviewed;         293 AA.
AC   Q724M3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 87.
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=LMOf2365_0201;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy
CC       group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
CC       {ECO:0000255|HAMAP-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
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 3/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00061}.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00061}.
DR   EMBL; AE017262; AAT02988.1; -; Genomic_DNA.
DR   RefSeq; WP_003725506.1; NC_002973.6.
DR   SMR; Q724M3; -.
DR   PRIDE; Q724M3; -.
DR   EnsemblBacteria; AAT02988; AAT02988; LMOf2365_0201.
DR   KEGG; lmf:LMOf2365_0201; -.
DR   HOGENOM; HOG000019600; -.
DR   KO; K00919; -.
DR   OMA; RWPSPAK; -.
DR   BioCyc; LMON265669:G1G0V-200-MONOMER; -.
DR   UniPathway; UPA00056; UER00094.
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: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;
DR   PRODOM; Q724M3.
DR   SWISS-2DPAGE; Q724M3.
KW   ATP-binding; Isoprene biosynthesis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    293       4-diphosphocytidyl-2-C-methyl-D-
FT                                erythritol kinase.
FT                                /FTId=PRO_0000189231.
FT   NP_BIND      94    104       ATP. {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE     10     10       {ECO:0000255|HAMAP-Rule:MF_00061}.
FT   ACT_SITE    136    136       {ECO:0000255|HAMAP-Rule:MF_00061}.
SQ   SEQUENCE   293 AA;  32203 MW;  7915EE91538AA06D CRC64;
     MKISITAPAK INLSLDALYK REDGYHEVEM VMTTIDLADR LYLERLDEDK IVLDVKAHFI
     PEDRRNLIYQ AALLLKKRFD VKMGVRITID KHIPVSAGLA GGSSDAAAAL KGLNVIWELG
     LSIEELAEIS SEIGSDIAFC VYGGTALATG RGEKISALPN IPGCWIVLAK PSISVSTPTI
     YKELQVDNVE HPDTQKMIES IKNGDLDGIF ASTGNVLESV TLEKNPQVKR IKDRMLAFGA
     EAALMSGSGP TVFALIKQYS RAKRVYNGLR GFCEEVYMVR PWSEGENDTN INN
//

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