ID ISPF_ECOSE Reviewed; 159 AA. AC B6I6D6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 85. DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECDP-synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECPP-synthase {ECO:0000255|HAMAP-Rule:MF_00107}; DE Short=MECPS {ECO:0000255|HAMAP-Rule:MF_00107}; DE EC=4.6.1.12 {ECO:0000255|HAMAP-Rule:MF_00107}; GN Name=ispF {ECO:0000255|HAMAP-Rule:MF_00107}; OrderedLocusNames=ECSE_2998; OS Escherichia coli (strain SE11). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=409438; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SE11; RX PubMed=18931093; DOI=10.1093/dnares/dsn026; RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.; RT "Complete genome sequence and comparative analysis of the wild-type RT commensal Escherichia coli strain SE11 isolated from a healthy adult."; RL DNA Res. 15:375-386(2008). 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). {ECO:0000255|HAMAP-Rule:MF_00107}. 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_00107}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00107}; CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00107}; 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_00107}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00107}. CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000255|HAMAP- CC Rule:MF_00107}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP009240; BAG78522.1; -; Genomic_DNA. DR RefSeq; WP_001219242.1; NC_011415.1. DR AlphaFoldDB; B6I6D6; -. DR SMR; B6I6D6; -. DR GeneID; 75205605; -. DR KEGG; ecy:ECSE_2998; -. DR HOGENOM; CLU_084630_2_0_6; -. DR UniPathway; UPA00056; UER00095. DR Proteomes; UP000008199; Chromosome. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase 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; cd00554; MECDP_synthase; 1. DR Gene3D; 3.30.1330.50; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; 1. DR HAMAP; MF_00107; IspF; 1. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. DR InterPro; IPR036571; MECDP_synthase_sf. DR NCBIfam; TIGR00151; ispF; 1. DR PANTHER; PTHR43181; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR43181:SF1; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; IpsF-like; 1. DR PROSITE; PS01350; ISPF; 1. PE 3: Inferred from homology; KW Isoprene biosynthesis; Lyase; Metal-binding. FT CHAIN 1..159 FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate FT synthase" FT /id="PRO_1000094261" FT BINDING 8..10 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 8 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 10 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 34..35 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 42 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 56..58 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 61..65 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 100..106 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 132..135 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 139 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT BINDING 142 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT SITE 34 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" FT SITE 133 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00107" SQ SEQUENCE 159 AA; 16898 MW; 9FC5563623A62939 CRC64; MRIGHGFDVH AFGGEGPIII GGVRIPYEKG LLAHSDGDVA LHALTDALLG AAALGDIGKL FPDTDPAFKG ADSRELLREA WRRIQAKGYT LGNVDVTIIA QAPKMLPHIP QMRVFIAEDL GCHMDDVNVK ATTTEKLGFT GRGEGIACEA VALLIKATK //