AC MF_00107; DC Protein; auto TR HAMAP; MF_00107; -; 1; level=0 XX Names: IspF XX ID ISPF 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=ispF; XX CC -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) CC and dimethylallyl diphosphate (DMAPP), two major building blocks of CC isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- CC C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol CC 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine CC 5-monophosphate (CMP). 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 Note=Binds 1 divalent metal cation per subunit.; 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 -!- SUBUNIT: Homotrimer. CC -!- SIMILARITY: Belongs to the IspF family. XX DR Pfam; PF02542; YgbB; 1; trigger=no DR NCBIfam; TIGR00151; IspF; 1; trigger=no DR PROSITE; PS01350; ISPF; 1; trigger=no XX KW Isoprene biosynthesis KW Lyase KW Metal-binding XX GO GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity GO GO:0016114; P:terpenoid biosynthetic process XX FT From: ISPF_ECOLI (P62617) FT BINDING 8..10 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: D-x-H FT BINDING 34..35 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: H-S FT BINDING 56..58 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: [DNEK]-[IVL]-[GA] FT BINDING 61..65 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: F-x-[DNEQ]-x-[DNEQ] FT BINDING 100..106 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: [ALVI]-x(2)-P-[KNR]-M-[LAGI] FT BINDING 132..135 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: [TS]-[TS]-x-[EDN] FT BINDING 8 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Condition: D FT BINDING 10 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Condition: H FT BINDING 42 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Condition: H FT BINDING 139 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: F FT BINDING 142 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT Condition: [RHK] FT SITE 34 FT /note="Transition state stabilizer" FT Condition: [HDN] FT SITE 133 FT /note="Transition state stabilizer" FT Condition: [TS] XX Size: 152-184; Related: MF_01520!; Template: P62617; P44815; Q8RQP5; P9WKG5; Q63T71; Q3JRA0; Q06756; Q5NFU1; Q8ZMF7; Q8EBR3; Q8ZBP7; Scope: Bacteria Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: See MF_01520 for bifunctional ispDF XX # Revision 1.40 2023/06/01 //