AC   MF_01520;
DC   Protein; auto
TR   HAMAP; MF_01520; -; 1; level=0
XX
Names: IspDF
XX
ID   ISPDF
DE   RecName: Full=Bifunctional enzyme IspD/IspF;
DE   Includes:
DE     RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
DE              EC=2.7.7.60;
DE     AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase;
DE     AltName: Full=MEP cytidylyltransferase;
DE              Short=MCT;
DE   Includes:
DE     RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase;
DE              Short=MECPP-synthase;
DE              Short=MECDP-synthase;
DE              Short=MECPS;
DE              EC=4.6.1.12;
GN   Name=ispDF;
XX
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).
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   -!- 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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 2/6.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 4/6.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI
CC       cytidylyltransferase family. IspD subfamily.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the IspF family.
XX
DR   Pfam; PF01128; IspD; 1; trigger=no
DR   Pfam; PF02542; YgbB; 1; trigger=no
DR   NCBIfam; TIGR00453; IspD; 1; trigger=no
DR   NCBIfam; TIGR00151; IspF; 1; trigger=no
DR   PROSITE; PS01295; ISPD; 1; trigger=no
DR   PROSITE; PS01350; ISPF; 1; trigger=no
XX
KW   Isoprene biosynthesis
KW   Lyase
KW   Metal-binding
KW   Multifunctional enzyme
KW   Nucleotidyltransferase
KW   Transferase
XX
GO   GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
GO   GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
GO   GO:0016114; P:terpenoid biosynthetic process
XX
FT   From: ISPDF_CAMJE (Q9PM68)
FT   REGION          Nter..210
FT                   /note="2-C-methyl-D-erythritol 4-phosphate
FT                   cytidylyltransferase"
FT   REGION          211..Cter
FT                   /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT                   synthase"
FT   BINDING         217..219
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: D-x-H
FT   BINDING         243..244
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: H-S
FT   BINDING         265..267
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: D-[IL]-G
FT   BINDING         270..274
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: [FY]-x-D-x-[DNE]
FT   BINDING         309..315
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: [AL]-x(2)-P-[KR]-M-[LAG]
FT   BINDING         341..344
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: [TS]-[T]-x-[ED]
FT   BINDING         217
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: D
FT   BINDING         219
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         251
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         348
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: [FY]
FT   BINDING         351
FT                   /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57919"
FT   Condition: [RK]
FT   SITE            16
FT                   /note="Transition state stabilizer"
FT   Condition: R
FT   SITE            23
FT                   /note="Transition state stabilizer"
FT   Condition: K
FT   SITE            139
FT                   /note="Positions MEP for the nucleophilic attack"
FT   Condition: [RH]
FT   SITE            191
FT                   /note="Positions MEP for the nucleophilic attack"
FT   Condition: K
FT   SITE            243
FT                   /note="Transition state stabilizer"
FT   Condition: [HDN]
FT   SITE            342
FT                   /note="Transition state stabilizer"
FT   Condition: [TS]
XX
Size: 359-422;
Related: MF_00107; MF_00108;
Template: Q9PM68; Q46893; P62617;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: See MF_00108 and MF_00107 for monofunctional ispD and ispF
XX
# Revision 1.35 2023/06/01
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