ID   ISPD_BORPD              Reviewed;         224 AA.
AC   A9II44;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   28-JAN-2026, entry version 80.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108};
GN   OrderedLocusNames=Bpet1695;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448 / CIP
OS   107267 / Se-1111R).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448 / CIP 107267 / Se-1111R;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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:0000255|HAMAP-Rule:MF_00108}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00108};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00108}.
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DR   EMBL; AM902716; CAP42034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9II44; -.
DR   SMR; A9II44; -.
DR   STRING; 94624.Bpet1695; -.
DR   KEGG; bpt:Bpet1695; -.
DR   eggNOG; COG1211; Bacteria.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000001225; 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-UniRule.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   FunFam; 3.90.550.10:FF:000003; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR050088; IspD/TarI_cytidylyltransf_bact.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR00453; ispD; 1.
DR   PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..224
FT                   /note="2-C-methyl-D-erythritol 4-phosphate
FT                   cytidylyltransferase"
FT                   /id="PRO_1000094311"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            25
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            154
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            210
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
SQ   SEQUENCE   224 AA;  23029 MW;  B763EB9841D5980A CRC64;
     MTDSLIAIVP AAGVGQRAGR PDLPKQYRLL AGQPMLRWAV AALLADARIG QVRVAVSPGD
     ERAGAALAGL PRTVCRPCGG PTRAATVAAA LADSNAADSD WILVHDAARP GLPPDALARL
     IDACLADAVG GLLALPVADT VKAGGPRVRA TLDRDGLWLA QTPQMFRAGV LRAALAAAQA
     GGGTVTDEAS AIEAAGHAPL LVPGAMRNFK VTWPDDFELM EKWL
//