ISPD_CHLPN
ID ISPD_CHLPN Reviewed; 211 AA.
AC Q9Z7X5; Q9JQI1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 136.
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=CPn_0579, CP_0169, CpB0603;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD18718.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38046.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98786.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98532.1; -; Genomic_DNA.
DR PIR; H72061; H72061.
DR PIR; H86562; H86562.
DR RefSeq; NP_224775.1; NC_000922.1.
DR RefSeq; WP_010883217.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z7X5; -.
DR SMR; Q9Z7X5; -.
DR STRING; 115711.CP_0169; -.
DR EnsemblBacteria; AAD18718; AAD18718; CPn_0579.
DR EnsemblBacteria; AAF38046; AAF38046; CP_0169.
DR GeneID; 45050623; -.
DR KEGG; cpa:CP_0169; -.
DR KEGG; cpj:yacM; -.
DR KEGG; cpn:CPn_0579; -.
DR KEGG; cpt:CpB0603; -.
DR PATRIC; fig|115713.3.peg.645; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_2_0; -.
DR OrthoDB; 1836139at2; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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..211
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000075561"
FT SITE 16
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 23
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 141
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 23447 MW; 412CB4DAA58C84B7 CRC64;
MIKSSLILLS GGQGTRFGSK IPKQYLPLNG TPLVLHSLKI LSSLPQIAEV IVVCDPSYQE
TFQEYPVSFA IPGERRQDSV FSGLQQVSYP WVIIHDGARP FIYPDEIHDL LETAEKIGAT
ALASPIPYTI KQRNPVRTLD RDNLAIIHTP QCIKTEILRE GLALAKEKQL TLVDDIEAAE
IIGKPSQLVF NKHPQIKISY PEDLTIAQAL L
