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Database: UniProt
Entry: A0A1T5EVH2_9FIRM
LinkDB: A0A1T5EVH2_9FIRM
Original site: A0A1T5EVH2_9FIRM 
ID   A0A1T5EVH2_9FIRM        Unreviewed;       233 AA.
AC   A0A1T5EVH2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000256|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000256|HAMAP-Rule:MF_00108};
GN   ORFNames=SAMN06296386_107148 {ECO:0000313|EMBL:SKB87848.1};
OS   Lachnospiraceae bacterium.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1898203 {ECO:0000313|EMBL:SKB87848.1, ECO:0000313|Proteomes:UP000191179};
RN   [1] {ECO:0000313|EMBL:SKB87848.1, ECO:0000313|Proteomes:UP000191179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1P17 {ECO:0000313|EMBL:SKB87848.1,
RC   ECO:0000313|Proteomes:UP000191179};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00108}.
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DR   EMBL; FUZG01000007; SKB87848.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5EVH2; -.
DR   OrthoDB; 9806837at2; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000191179; Unassembled WGS sequence.
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   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR00453; ispD; 1.
DR   PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00108};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00108}; Reference proteome {ECO:0000313|Proteomes:UP000191179};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00108}.
FT   SITE            15
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            22
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            153
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            217
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ   SEQUENCE   233 AA;  26298 MW;  C7EB3E242CA69EFF CRC64;
     MKTQAIVLAG GKGRRMGGAT PKQYLMLKDK PVLYYSLRAF EDSFIDEVIL VCGEGEEEYC
     RKEIVLKYGF TKVVKIVSGG RERFDSVYNG LEASDGCDYV YIHDGARPLV SQYILERCQH
     YVEKYRAAVA GAKAKDTIKM DNGDGFIEST PDRDRMWLMQ TPQVFEYGLI KTCYEKLIQD
     RERLASAGVN VTDDTMVAKM YGNIDAKLVE NPDPNLKITT PEDLKIAGFL LDK
//
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