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ISPF_ECODH
ID   ISPF_ECODH              Reviewed;         159 AA.
AC   B1XCS2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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};
GN   OrderedLocusNames=ECDH10B_2914;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(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}.
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DR   EMBL; CP000948; ACB03863.1; -; Genomic_DNA.
DR   RefSeq; WP_001219242.1; NC_010473.1.
DR   AlphaFoldDB; B1XCS2; -.
DR   SMR; B1XCS2; -.
DR   GeneID; 67413962; -.
DR   KEGG; ecd:ECDH10B_2914; -.
DR   HOGENOM; CLU_084630_2_0_6; -.
DR   OMA; QHFGTGR; -.
DR   BioCyc; ECOL316385:ECDH10B_RS14800-MON; -.
DR   UniPathway; UPA00056; UER00095.
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; -; 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   PANTHER; PTHR43181; PTHR43181; 1.
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   Isoprene biosynthesis; Lyase; Metal-binding.
FT   CHAIN           1..159
FT                   /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT                   synthase"
FT                   /id="PRO_1000094260"
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
 
 
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