ISPD_YERPS
ID ISPD_YERPS Reviewed; 241 AA.
AC Q66EC3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=YPTB0770;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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 -!- SUBUNIT: Homodimer. {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; BX936398; CAH20010.1; -; Genomic_DNA.
DR RefSeq; WP_011191776.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66EC3; -.
DR SMR; Q66EC3; -.
DR EnsemblBacteria; CAH20010; CAH20010; YPTB0770.
DR GeneID; 66842809; -.
DR KEGG; ypo:BZ17_1786; -.
DR KEGG; yps:YPTB0770; -.
DR PATRIC; fig|273123.14.peg.1891; -.
DR OMA; ERQHSVY; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000001011; 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..241
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000075654"
FT SITE 23
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 30
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 160
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 216
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
SQ SEQUENCE 241 AA; 26399 MW; 16B81BF1573CA31E CRC64;
MSNFAVSLPE VIAVLPAAGI GSRMLADCPK QYLTVGGKTI IEHAIFSLLH HPRIQRVIVV
IHPQDTQFSR LSVAQDPRIS TVYGGDQRAN SVMAGLQLAG QAEWVLVHDA ARPCLHLDDL
SRLLSITECS QVGGILAAPV RDTMKRAEPG IQAIAHTVDR QDLWHALTPQ LFPLELLKLC
LSRALREGVA VTDEASALEY CGYHPILVTG RSDNIKVTRP EDLALAEFYL TQRQSLNNDS
L
