ISPD_THEP1
ID ISPD_THEP1 Reviewed; 222 AA.
AC A5IMI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Tpet_1390;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) 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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000702; ABQ47404.1; -; Genomic_DNA.
DR RefSeq; WP_011943863.1; NC_009486.1.
DR AlphaFoldDB; A5IMI1; -.
DR SMR; A5IMI1; -.
DR STRING; 390874.Tpet_1390; -.
DR EnsemblBacteria; ABQ47404; ABQ47404; Tpet_1390.
DR KEGG; tpt:Tpet_1390; -.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_061281_2_2_0; -.
DR OMA; ERQHSVY; -.
DR UniPathway; UPA00056; UER00093.
DR Proteomes; UP000006558; 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..222
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_1000022956"
FT SITE 14
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 21
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 149
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT SITE 201
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
SQ SEQUENCE 222 AA; 25388 MW; 4C1283E81078A9FD CRC64;
MNVAILLAAG KGERMSENVP KQFLEIEGRM LFEYPLSTFL KSEAIDGVVI VTRREWFEVV
EKRVFHEKVL GIVEGGDTRS QSVRSALEFL EKFSPSYVLV HDSARPFLRK KHVSEVLRRA
RETGAATLAL KNSDALVRVE NDRMEYIPRK GVYRILTPQA FSYEILKKAH ENGGEWADDT
EPVQKLGVKI ALVEGDPLCF KVTFKEDLEL ARIIAREWER IP
