ID   ISPD_NEOSM              Reviewed;         232 AA.
AC   Q2GEM3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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}; OrderedLocusNames=NSE_0178;
OS   Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS   sennetsu).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=222891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-367 / Miyayama;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000237; ABD46254.1; -; Genomic_DNA.
DR   RefSeq; WP_011451579.1; NC_007798.1.
DR   AlphaFoldDB; Q2GEM3; -.
DR   SMR; Q2GEM3; -.
DR   STRING; 222891.NSE_0178; -.
DR   EnsemblBacteria; ABD46254; ABD46254; NSE_0178.
DR   KEGG; nse:NSE_0178; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_2_2_5; -.
DR   OMA; ERQHSVY; -.
DR   OrthoDB; 1836139at2; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000001942; 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; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; SSF53448; 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_1000202893"
FT   SITE            16
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            24
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            156
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            213
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
SQ   SEQUENCE   232 AA;  25310 MW;  C3794CA36EA09DE3 CRC64;
     MGKIAGLVVA GGGGSRITNS VLPKQYLQVR GKAILQYTVE ALFAHPKIEC VHLVVNSKCE
     VHYLPILRNL SGYVVSLSEA GNTRTDSVFS GLKALECLNP SHVLIQDAAR PFTTPKVINA
     VIKSLLEGCE GVVPVVPVQD TIIKREPEGI VTDVNRDELR IVQTPQGFDF CKIFAAYKAH
     FMCPSKRYTD DGSLALAHGI KVECIPGDSS NLKITHPFDL KFADFLLAQS HR