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 19-FEB-2014, entry version 44. DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; DE Short=MECDP-synthase; DE Short=MECPP-synthase; DE Short=MECPS; DE EC=4.6.1.12; GN Name=ispF; OrderedLocusNames=ECSE_2998; OS Escherichia coli (strain SE11). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 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., RA Ooka T., 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 RT adult."; RL DNA Res. 15:375-386(2008). CC -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate CC (IPP) and dimethylallyl diphosphate (DMAPP), two major building CC blocks of isoprenoid compounds. Catalyzes the conversion of 4- CC diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to CC 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a CC corresponding release of cytidine 5-monophosphate (CMP) (By CC similarity). CC -!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C- CC methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate CC + CMP. CC -!- COFACTOR: Binds 1 divalent metal cation per subunit (By CC similarity). CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 4/6. CC -!- SUBUNIT: Homotrimer (By similarity). CC -!- SIMILARITY: Belongs to the IspF family. 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; YP_002294273.1; NC_011415.1. DR ProteinModelPortal; B6I6D6; -. DR SMR; B6I6D6; 1-156. DR STRING; 409438.ECSE_2998; -. DR BindingDB; B6I6D6; -. DR EnsemblBacteria; BAG78522; BAG78522; ECSE_2998. DR GeneID; 7001383; -. DR KEGG; ecy:ECSE_2998; -. DR PATRIC; 18424600; VBIEscCol83070_3168. DR eggNOG; COG0245; -. DR HOGENOM; HOG000239175; -. DR KO; K01770; -. DR OMA; HKFGGEG; -. DR OrthoDB; EOG6J48RZ; -. DR ProtClustDB; PRK00084; -. DR BioCyc; ECOL409438:GHUU-3054-MONOMER; -. DR UniPathway; UPA00056; UER00095. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-HAMAP. 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-HAMAP. DR Gene3D; 3.30.1330.50; -; 1. DR HAMAP; MF_00107; IspF; 1. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; SSF69765; 1. DR TIGRFAMs; TIGR00151; ispF; 1. DR PROSITE; PS01350; ISPF; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding. FT CHAIN 1 159 2-C-methyl-D-erythritol 2,4- FT cyclodiphosphate synthase. FT /FTId=PRO_1000094261. FT REGION 8 10 Substrate binding (By similarity). FT REGION 34 35 Substrate binding (By similarity). FT REGION 38 46 Substrate binding (By similarity). FT REGION 56 58 Substrate binding (By similarity). FT REGION 61 65 Substrate binding (By similarity). FT REGION 100 106 Substrate binding (By similarity). FT REGION 131 135 Substrate binding (By similarity). FT METAL 8 8 Divalent metal cation (By similarity). FT METAL 10 10 Divalent metal cation (By similarity). FT METAL 42 42 Divalent metal cation (By similarity). FT BINDING 65 65 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 139 139 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 142 142 Substrate (By similarity). FT SITE 34 34 Transition state stabilizer (By FT similarity). FT SITE 133 133 Transition state stabilizer (By FT similarity). SQ SEQUENCE 159 AA; 16898 MW; 9FC5563623A62939 CRC64; MRIGHGFDVH AFGGEGPIII GGVRIPYEKG LLAHSDGDVA LHALTDALLG AAALGDIGKL FPDTDPAFKG ADSRELLREA WRRIQAKGYT LGNVDVTIIA QAPKMLPHIP QMRVFIAEDL GCHMDDVNVK ATTTEKLGFT GRGEGIACEA VALLIKATK //