ISPDF_CAMJE
ID ISPDF_CAMJE Reviewed; 371 AA.
AC Q9PM68; Q0P821;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Bifunctional enzyme IspD/IspF {ECO:0000255|HAMAP-Rule:MF_01520};
DE Includes:
DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_01520};
DE EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_01520};
DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_01520};
DE AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_01520};
DE Short=MCT {ECO:0000255|HAMAP-Rule:MF_01520};
DE Includes:
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01520};
DE Short=MECDP-synthase {ECO:0000255|HAMAP-Rule:MF_01520};
DE Short=MECPP-synthase {ECO:0000255|HAMAP-Rule:MF_01520};
DE Short=MECPS {ECO:0000255|HAMAP-Rule:MF_01520};
DE EC=4.6.1.12 {ECO:0000255|HAMAP-Rule:MF_01520};
GN Name=ispDF {ECO:0000255|HAMAP-Rule:MF_01520}; OrderedLocusNames=Cj1607;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP PROTEIN SEQUENCE OF 1-22, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15233799; DOI=10.1111/j.1432-1033.2004.04234.x;
RA Gabrielsen M., Rohdich F., Eisenreich W., Graewert T., Hecht S., Bacher A.,
RA Hunter W.N.;
RT "Biosynthesis of isoprenoids. A bifunctional IspDF enzyme from
RT Campylobacter jejuni.";
RL Eur. J. Biochem. 271:3028-3035(2004).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the formation of 4-
CC diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-
CC erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-
CC diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-
CC methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding
CC release of cytidine 5-monophosphate (CMP) (IspF). {ECO:0000255|HAMAP-
CC Rule:MF_01520, ECO:0000269|PubMed:15233799}.
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_01520,
CC ECO:0000269|PubMed:15233799};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-
CC erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01520,
CC ECO:0000269|PubMed:15233799};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01520,
CC ECO:0000269|PubMed:15233799};
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_01520}.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 4/6. {ECO:0000255|HAMAP-Rule:MF_01520}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI
CC cytidylyltransferase family. IspD subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01520}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the IspF family.
CC {ECO:0000255|HAMAP-Rule:MF_01520}.
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DR EMBL; AL111168; CAL35704.1; -; Genomic_DNA.
DR PIR; E81256; E81256.
DR RefSeq; WP_002851397.1; NC_002163.1.
DR RefSeq; YP_002344976.1; NC_002163.1.
DR PDB; 1W55; X-ray; 2.30 A; A=1-371.
DR PDB; 1W57; X-ray; 3.09 A; A=1-371.
DR PDBsum; 1W55; -.
DR PDBsum; 1W57; -.
DR AlphaFoldDB; Q9PM68; -.
DR SMR; Q9PM68; -.
DR IntAct; Q9PM68; 27.
DR STRING; 192222.Cj1607; -.
DR DrugBank; DB03403; Cytidine-5'-Monophosphate.
DR DrugBank; DB02552; Geranyl Diphosphate.
DR PaxDb; Q9PM68; -.
DR PRIDE; Q9PM68; -.
DR EnsemblBacteria; CAL35704; CAL35704; Cj1607.
DR GeneID; 905874; -.
DR KEGG; cje:Cj1607; -.
DR PATRIC; fig|192222.6.peg.1583; -.
DR eggNOG; COG0245; Bacteria.
DR eggNOG; COG1211; Bacteria.
DR HOGENOM; CLU_042800_2_5_7; -.
DR OMA; TGYDVHA; -.
DR UniPathway; UPA00056; UER00093.
DR UniPathway; UPA00056; UER00095.
DR EvolutionaryTrace; Q9PM68; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 CDD; cd00554; MECDP_synthase; 1.
DR Gene3D; 3.30.1330.50; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01520; IspDF; 1.
DR HAMAP; MF_00107; IspF; 1.
DR InterPro; IPR001228; IspD.
DR InterPro; IPR026596; IspD/F.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR018294; ISPD_synthase_CS.
DR InterPro; IPR003526; MECDP_synthase.
DR InterPro; IPR020555; MECDP_synthase_CS.
DR InterPro; IPR036571; MECDP_synthase_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43181; PTHR43181; 1.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF02542; YgbB; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF69765; SSF69765; 1.
DR TIGRFAMs; TIGR00453; ispD; 1.
DR TIGRFAMs; TIGR00151; ispF; 1.
DR PROSITE; PS01295; ISPD; 1.
DR PROSITE; PS01350; ISPF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isoprene biosynthesis; Lyase;
KW Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..371
FT /note="Bifunctional enzyme IspD/IspF"
FT /id="PRO_0000075662"
FT REGION 1..210
FT /note="2-C-methyl-D-erythritol 4-phosphate
FT cytidylyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01520"
FT REGION 211..371
FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT synthase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01520"
FT BINDING 217..219
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 217
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 219
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 243..244
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 251
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 265..267
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 270..274
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 309..315
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 341..344
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 348
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT BINDING 351
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT SITE 16
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01520"
FT SITE 23
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01520"
FT SITE 139
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01520"
FT SITE 191
FT /note="Positions MEP for the nucleophilic attack"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01520"
FT SITE 243
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT SITE 342
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62617, ECO:0000255|HAMAP-
FT Rule:MF_01520"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1W55"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:1W55"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 210..225
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1W57"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1W57"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 298..308
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:1W55"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:1W55"
FT STRAND 353..365
FT /evidence="ECO:0007829|PDB:1W55"
SQ SEQUENCE 371 AA; 41690 MW; BAD0087B19905FAF CRC64;
MSEMSLIMLA AGNSTRFNTK VKKQFLRLGN DPLWLYATKN LSSFYPFKKI VVTSSNITYM
KKFTKNYEFI EGGDTRAESL KKALELIDSE FVMVSDVARV LVSKNLFDRL IENLDKADCI
TPALKVADTT LFDNEALQRE KIKLIQTPQI SKTKLLKKAL DQNLEFTDDS TAIAAMGGKI
WFVEGEENAR KLTFKEDLKK LDLPTPSFEI FTGNGFDVHE FGENRPLLLA GVQIHPTMGL
KAHSDGDVLA HSLTDAILGA AGLGDIGELY PDTDMKFKNA NSMELLKQAY DKVREIGFEL
INIDICVMAQ SPKLKDFKQA MQSNIAHTLD LDEFRINVKA TTTEKLGFIG RKEGMAVLSS
VNLKYFDWTR L
