ID   Q2KUX3_BORA1            Unreviewed;       228 AA.
AC   Q2KUX3;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   02-APR-2025, entry version 117.
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   ECO:0000313|EMBL:CAJ48669.1};
GN   OrderedLocusNames=BAV1060 {ECO:0000313|EMBL:CAJ48669.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ48669.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ48669.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ48669.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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|ARBA:ARBA00001282, ECO:0000256|HAMAP-
CC         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|ARBA:ARBA00004787, ECO:0000256|HAMAP-
CC       Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000256|ARBA:ARBA00009789, ECO:0000256|HAMAP-
CC       Rule:MF_00108}.
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DR   EMBL; AM167904; CAJ48669.1; -; Genomic_DNA.
DR   RefSeq; WP_012416744.1; NC_010645.1.
DR   AlphaFoldDB; Q2KUX3; -.
DR   STRING; 360910.BAV1060; -.
DR   GeneID; 92935746; -.
DR   KEGG; bav:BAV1060; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_3_0_4; -.
DR   OrthoDB; 9806837at2; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000001977; 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-UniRule.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   FunFam; 3.90.550.10:FF:000003; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR050088; IspD/TarI_cytidylyltransf_bact.
DR   InterPro; IPR018294; ISPD_synthase_CS.
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.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW   Rule:MF_00108};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00108}; Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00108}.
FT   SITE            18
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            29
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            158
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            214
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ   SEQUENCE   228 AA;  24105 MW;  BA993A08D9C165CA CRC64;
     MKSEPLIAIV PAAGVGSRAS QPGQEAVPKQ YRTLNGQPML RRAVLALLAD ARIGQVRVAV
     SAGDDWAAEA LRGLPRTLWR PCGGPTRADT VAAALDDAAL APETWVLVHD AARPGLPADA
     LARLIDGCLD DAVGGLLALP VADTVKSGAA RVRATLDRDG LWLAQTPQMF RAGMLRHALQ
     TAREQGLPVT DEASAIEAQG LSPRLIGGSA RNFKVTWPDD FALMEKWL
//