ID   ISPE_SOLLC              Reviewed;         401 AA.
AC   P93841;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase, chloroplastic/chromoplastic;
DE            EC=2.7.1.148;
DE   AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
DE            Short=CMK;
DE   AltName: Full=Ripening-associated protein pTOM41;
DE   Flags: Precursor; Fragment;
GN   Name=ISPE;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9049268; DOI=10.1023/a:1005785321165;
RA   Lawrence S.D., Cline K., Moore G.A.;
RT   "Chromoplast development in ripening tomato fruit: identification of cDNAs
RT   for chromoplast-targeted proteins and characterization of a cDNA encoding a
RT   plastid-localized low-molecular-weight heat shock protein.";
RL   Plant Mol. Biol. 33:483-492(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 81-401, AND CHARACTERIZATION.
RX   PubMed=10880567; DOI=10.1073/pnas.140209197;
RA   Rohdich F., Wungsintaweekul J., Luettgen H., Fischer M., Eisenreich W.,
RA   Schuhr C.A., Fellermeier M., Schramek N., Zenk M.H., Bacher A.;
RT   "Biosynthesis of terpenoids: 4-diphosphocytidyl-2-C-methyl-D-erythritol
RT   kinase from tomato.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:8251-8256(2000).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC       of 4-diphosphocytidyl-2C-methyl-D-erythritol.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Divalent metal ions. Preferably magnesium.;
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. Plastid,
CC       chromoplast.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF76143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U62773; AAB49936.1; -; Genomic_DNA.
DR   EMBL; AF258339; AAF76143.1; ALT_INIT; mRNA.
DR   EMBL; AF263101; AAF87717.1; -; mRNA.
DR   PIR; T07419; T07419.
DR   AlphaFoldDB; P93841; -.
DR   SMR; P93841; -.
DR   STRING; 4081.Solyc01g009010.2.1; -.
DR   BindingDB; P93841; -.
DR   ChEMBL; CHEMBL2285352; -.
DR   PaxDb; P93841; -.
DR   PRIDE; P93841; -.
DR   eggNOG; ENOG502QT9C; Eukaryota.
DR   InParanoid; P93841; -.
DR   BioCyc; MetaCyc:MON-11959; -.
DR   BRENDA; 2.7.1.148; 3101.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P93841; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   HAMAP; MF_00061; IspE; 1.
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; PF00288; GHMP_kinases_N; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
DR   TIGRFAMs; TIGR00154; ispE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chloroplast; Chromoplast; Isoprene biosynthesis; Kinase;
KW   Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..88
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           89..401
FT                   /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase,
FT                   chloroplastic/chromoplastic"
FT                   /id="PRO_0000016480"
FT   BINDING         181..191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   401 AA;  44527 MW;  9B5E265281561192 CRC64;
     LWLPVIFFVV SNPKLILLKR VVFFQSWSNR PHGSSYFNKN IQFRRNSFVI VKASGSRTSK
     KQVEITYNPE EKFNKLADEV DREAGLSRLT LFSPCKINVF LRITSKRDDG YHDLASLFHV
     ISLGDKIKFS LSPSKSKDRL STNVAGVPLD ERNLIIKALN LYRKKTGTDN YFWIHLDKKV
     PTGAGLGGGS SNAATTLWAA NQFSGCVATE KELQEWSGEI GSDIPFFFSH GAAYCTGRGE
     VVQDIPSPIP FDIPMVLIKP QQACSTAEVY KRFQLDLSSK VDPLSLLEKI STSGISQDVC
     VNDLEPPAFE VLPSLKRLKQ RVIAAGRGQY DAVFMSGSGS TIVGVGSPDP PQFVYDDEEY
     KDVFLSEASF ITRPANEWYV EPVSGSTIGD QPEFSTSFDM S