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ISPF_CUPPJ
ID   ISPF_CUPPJ              Reviewed;         169 AA.
AC   Q472F1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Reut_A1362;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ60732.1; -; Genomic_DNA.
DR   RefSeq; WP_011297532.1; NC_007347.1.
DR   AlphaFoldDB; Q472F1; -.
DR   SMR; Q472F1; -.
DR   STRING; 264198.Reut_A1362; -.
DR   EnsemblBacteria; AAZ60732; AAZ60732; Reut_A1362.
DR   KEGG; reu:Reut_A1362; -.
DR   eggNOG; COG0245; Bacteria.
DR   HOGENOM; CLU_084630_2_0_4; -.
DR   OMA; QHFGTGR; -.
DR   OrthoDB; 1716560at2; -.
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..169
FT                   /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT                   synthase"
FT                   /id="PRO_0000237747"
FT   BINDING         13..15
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         13
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   BINDING         15
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   BINDING         39..40
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         47
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   BINDING         61..63
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         66..70
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         144
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         147
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            39
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   SITE            138
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
SQ   SEQUENCE   169 AA;  17882 MW;  C260FA2CC25F3B01 CRC64;
     MMPFDIRVGQ GYDVHALVPG RKLILGGVHI PHDRGLLGHS DADALLHAIT DALFGAAGLG
     DIGRHFPDTD AQFAGADSRV LLREAARRVR EAGYEIGNVD ASVIAQQPKL APHIPGMVAN
     IADDLGLPAT RCNVKAKTNE KLGFEGRQEG IVAQAAVLIW RGAIADAQD
 
 
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