ISPD_THEMA
ID ISPD_THEMA Reviewed; 222 AA.
AC Q9X1B3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 134.
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=TM_1393;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36464.1; -; Genomic_DNA.
DR PIR; B72259; B72259.
DR RefSeq; NP_229194.1; NC_000853.1.
DR RefSeq; WP_004081602.1; NZ_CP011107.1.
DR PDB; 1VPA; X-ray; 2.67 A; A/B=1-222.
DR PDBsum; 1VPA; -.
DR AlphaFoldDB; Q9X1B3; -.
DR SMR; Q9X1B3; -.
DR STRING; 243274.THEMA_07350; -.
DR DrugBank; DB02431; Cytidine-5'-Triphosphate.
DR EnsemblBacteria; AAD36464; AAD36464; TM_1393.
DR KEGG; tma:TM1393; -.
DR eggNOG; COG1211; Bacteria.
DR InParanoid; Q9X1B3; -.
DR OMA; ERQHSVY; -.
DR OrthoDB; 1836139at2; -.
DR UniPathway; UPA00056; UER00093.
DR EvolutionaryTrace; Q9X1B3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070567; F:cytidylyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /id="PRO_0000075638"
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"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:1VPA"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1VPA"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1VPA"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:1VPA"
SQ SEQUENCE 222 AA; 25370 MW; 51D5E945D078ACEC CRC64;
MNVAILLAAG KGERMSENVP KQFLEIEGRM LFEYPLSTFL KSEAIDGVVI VTRREWFEVV
EKRVFHEKVL GIVEGGDTRS QSVRSALEFL EKFSPSYVLV HDSARPFLRK KHVSEVLRRA
RETGAATLAL KNSDALVRVE NDRIEYIPRK GVYRILTPQA FSYEILKKAH ENGGEWADDT
EPVQKLGVKI ALVEGDPLCF KVTFKEDLEL ARIIAREWER IP
