(data stored in ACNUC7421 zone)

SWISSPROT: ISPF_FRASN

ID   ISPF_FRASN              Reviewed;         160 AA.
AC   A8LF85;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, 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=Franean1_0364;
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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).
CC       {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;
CC         EC=4.6.1.12; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00107};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000820; ABW09830.1; -; Genomic_DNA.
DR   RefSeq; WP_012157806.1; NC_009921.1.
DR   SMR; A8LF85; -.
DR   STRING; 298653.Franean1_0364; -.
DR   EnsemblBacteria; ABW09830; ABW09830; Franean1_0364.
DR   KEGG; fre:Franean1_0364; -.
DR   eggNOG; ENOG4108UH8; Bacteria.
DR   eggNOG; COG0245; LUCA.
DR   HOGENOM; HOG000239175; -.
DR   KO; K01770; -.
DR   OMA; DIGHYFP; -.
DR   OrthoDB; 1716560at2; -.
DR   BioCyc; FSP298653:G1G9X-361-MONOMER; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000001313; 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; IPR036571; MECDP_synthase_sf.
DR   Pfam; PF02542; YgbB; 1.
DR   SUPFAM; SSF69765; SSF69765; 1.
DR   TIGRFAMs; TIGR00151; ispF; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8LF85.
DR   SWISS-2DPAGE; A8LF85.
KW   Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    160       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT                                /FTId=PRO_1000094264.
FT   REGION       14     16       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       40     41       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       44     52       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       62     64       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION      134    138       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00107}.
FT   METAL        14     14       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00107}.
FT   METAL        16     16       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00107}.
FT   METAL        48     48       Divalent metal cation.
FT                                {ECO:0000255|HAMAP-Rule:MF_00107}.
FT   BINDING     145    145       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00107}.
FT   SITE         40     40       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00107}.
FT   SITE        136    136       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00107}.
SQ   SEQUENCE   160 AA;  16070 MW;  0BECA73961DA02F2 CRC64;
     MTEPSLPRVG TGVDVHPFEQ GRECWVACLL WPGETGLAGH SDGDVASHAA CDALLTASGI
     GDLGAVFGTG RPEWSGASGA ALLGETARLL AEGGWLIGNV AVQVVGNRPR MAARRVEAQE
     AMSAALGAPV NLSATTTDGL GLTGRGEGLA AIATALVTRV
//

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