ID   ISPD_LISMO              Reviewed;         232 AA.
AC   Q8YAB5;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
DE            EC=2.7.7.60;
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase;
DE   AltName: Full=MEP cytidylyltransferase;
DE            Short=MCT;
GN   Name=ispD; OrderedLocusNames=lmo0235;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-
CC       erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-
CC         methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60;
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 2/6.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL591974; CAD00762.1; -; Genomic_DNA.
DR   PIR; AD1104; AD1104.
DR   RefSeq; NP_463766.1; NC_003210.1.
DR   RefSeq; WP_010989381.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8YAB5; -.
DR   SMR; Q8YAB5; -.
DR   STRING; 169963.lmo0235; -.
DR   PaxDb; Q8YAB5; -.
DR   EnsemblBacteria; CAD00762; CAD00762; CAD00762.
DR   GeneID; 987220; -.
DR   KEGG; lmo:lmo0235; -.
DR   PATRIC; fig|169963.11.peg.243; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_2_2_9; -.
DR   OMA; ERQHSVY; -.
DR   PhylomeDB; Q8YAB5; -.
DR   BioCyc; LMON169963:LMO0235-MON; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IBA:GO_Central.
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   CDD; cd02516; CDP-ME_synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00453; ispD; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..232
FT                   /note="2-C-methyl-D-erythritol 4-phosphate
FT                   cytidylyltransferase"
FT                   /id="PRO_0000075587"
FT   SITE            15
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            22
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            153
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000250"
FT   SITE            209
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   232 AA;  25910 MW;  D8DEDEC6B391E969 CRC64;
     MNYELVFLAA GQGKRMNAQK NKMWLELVGE PIFIHALRPF LADNRCSKVI VVCQEEERKH
     VKELMSQLNV AEHRIEIVKG GSERQYSVAA GLERCGTGRV VLVHDGARPF ITLDIIDRLL
     IGVEQSKAAI CAVKVKDTVK RVMNGVVQET VDRENLWQVQ TPQAFELPIL RKAHQLARKE
     QFLGTDEASL VERIPCPVAI VQGSYYNIKL TTPEDMPLAK AILGELGGIA ND