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ISPF_IDILO
ID   ISPF_IDILO              Reviewed;         159 AA.
AC   Q5QUC4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=IL0751;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV81592.1; -; Genomic_DNA.
DR   RefSeq; WP_011234003.1; NC_006512.1.
DR   AlphaFoldDB; Q5QUC4; -.
DR   SMR; Q5QUC4; -.
DR   STRING; 283942.IL0751; -.
DR   EnsemblBacteria; AAV81592; AAV81592; IL0751.
DR   KEGG; ilo:IL0751; -.
DR   eggNOG; COG0245; Bacteria.
DR   HOGENOM; CLU_084630_2_0_6; -.
DR   OMA; QHFGTGR; -.
DR   OrthoDB; 1716560at2; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000001171; 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; -; 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; Reference proteome.
FT   CHAIN           1..159
FT                   /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT                   synthase"
FT                   /id="PRO_0000237732"
FT   BINDING         10..12
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         10
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   BINDING         12
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   BINDING         36..37
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         44
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   BINDING         58..60
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         63..67
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         102..108
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         134..137
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         141
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   SITE            36
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
FT   SITE            135
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00107"
SQ   SEQUENCE   159 AA;  17080 MW;  197B7285387BA6BC CRC64;
     MKIRVGHGYD VHRWGSDKPL ILGGVEIEHH QGLVAHSDGD VVLHAVTDAV LGALALGDIG
     QHFPDTDERY AGADSAELLS HAVSLCQEKE FKTGNIDVTI VAQAPKMAPH IDDMRSSIAQ
     CLKTCIDNVN VKATTTEKLG FVGREEGIAC HAVVLMESF
 
 
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