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Database: UniProt
Entry: B7JK94
LinkDB: B7JK94
Original site: B7JK94 
ID   ISPF_BACC0              Reviewed;         158 AA.
AC   B7JK94;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   01-MAY-2013, entry version 37.
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=BCAH820_0097;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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.
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DR   EMBL; CP001283; ACK88782.1; -; Genomic_DNA.
DR   RefSeq; YP_002449123.1; NC_011773.1.
DR   ProteinModelPortal; B7JK94; -.
DR   SMR; B7JK94; 3-158.
DR   STRING; 405535.BCAH820_0097; -.
DR   EnsemblBacteria; ACK88782; ACK88782; BCAH820_0097.
DR   GeneID; 7190338; -.
DR   KEGG; bcu:BCAH820_0097; -.
DR   PATRIC; 18836995; VBIBacCer122868_0095.
DR   eggNOG; COG0245; -.
DR   HOGENOM; HOG000239175; -.
DR   KO; K01770; -.
DR   OMA; HKFGGEG; -.
DR   ProtClustDB; PRK00084; -.
DR   BioCyc; BCER405535:GHSL-1955-MONOMER; -.
DR   UniPathway; UPA00056; UER00095.
DR   GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA: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; YgbB_synth; 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    158       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT                                /FTId=PRO_1000117417.
FT   REGION        9     11       Substrate binding (By similarity).
FT   REGION       35     36       Substrate binding (By similarity).
FT   REGION       39     47       Substrate binding (By similarity).
FT   REGION       57     59       Substrate binding (By similarity).
FT   REGION       62     66       Substrate binding (By similarity).
FT   REGION      101    107       Substrate binding (By similarity).
FT   REGION      132    136       Substrate binding (By similarity).
FT   METAL         9      9       Divalent metal cation (By similarity).
FT   METAL        11     11       Divalent metal cation (By similarity).
FT   METAL        43     43       Divalent metal cation (By similarity).
FT   BINDING      66     66       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     140    140       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     143    143       Substrate (By similarity).
FT   SITE         35     35       Transition state stabilizer (By
FT                                similarity).
FT   SITE        134    134       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   158 AA;  17219 MW;  CC61E2EB140C4824 CRC64;
     MFRIGQGFDV HEFAEGRPLI IGGITIPHEK GLIGHSDADV LLHTIADACL GAIAAGDIGK
     HFPDTDPAFK DADSAVLLQK VWEFVREQGY ELGNLDCTII AQKPKMAPHI ESMRKRISEL
     LETSIDNINV KATTTEKLGF TGREEGIASQ AVVLLQKK
//
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