ID   ISPD_LISIN              Reviewed;         232 AA.
AC   Q92F40;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=lin0267;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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; AL596164; CAC95500.1; -; Genomic_DNA.
DR   PIR; AD1466; AD1466.
DR   RefSeq; WP_010990302.1; NC_003212.1.
DR   AlphaFoldDB; Q92F40; -.
DR   SMR; Q92F40; -.
DR   STRING; 272626.lin0267; -.
DR   EnsemblBacteria; CAC95500; CAC95500; CAC95500.
DR   KEGG; lin:lin0267; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_2_2_9; -.
DR   OMA; ERQHSVY; -.
DR   OrthoDB; 1836139at2; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; 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   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; Transferase.
FT   CHAIN           1..232
FT                   /note="2-C-methyl-D-erythritol 4-phosphate
FT                   cytidylyltransferase"
FT                   /id="PRO_0000075583"
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;  26040 MW;  89BD8CB7D117B31D CRC64;
     MNYELIFLAA GQGKRMNAEK NKMWLDLVGE PIFIHALRPF LADNRCSKVI VVCQETERKH
     VRKLMQQLDV AEDRVEVVKG GSERQYSVAA GLECCGLESV VLVHDGARPF VTLDIIDRLL
     LGVKQNKAAI CAVQVKDTVK RVIHDVVKET VDRDNLWQIQ TPQAFELHIL QKAHRLAKKD
     QFLGTDEASL VERIPYPVAI VQGSYYNIKL TTPEDMPLAK AILGELGGKV ND