ISPF_PLAFX
ID ISPF_PLAFX Reviewed; 240 AA.
AC P62369; A0A0L7K7H5; O96178;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, apicoplast {ECO:0000303|PubMed:11389720};
DE Short=MECDP-synthase {ECO:0000305};
DE Short=MECPS {ECO:0000305};
DE EC=4.6.1.12 {ECO:0000269|PubMed:11389720};
DE Flags: Precursor;
GN Name=IspF {ECO:0000303|PubMed:11389720}; ORFNames=PFHG_00813;
OS Plasmodium falciparum (isolate HB3).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=137071;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=11389720; DOI=10.1046/j.1432-1327.2001.02204.x;
RA Rohdich F., Eisenreich W., Wungsintaweekul J., Hecht S., Schuhr C.A.,
RA Bacher A.;
RT "Biosynthesis of terpenoids. 2C-methyl-D-erythritol 2,4-cyclodiphosphate
RT synthase (IspF) from Plasmodium falciparum.";
RL Eur. J. Biochem. 268:3190-3197(2001).
RN [2] {ECO:0000312|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB3 {ECO:0000312|EMBL:KOB59060.1};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In the mevalonate-independent isoprenoid biosynthetic
CC pathway, converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate
CC into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP.
CC {ECO:0000269|PubMed:11389720}.
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:0000269|PubMed:11389720};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:11389720};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:P62368};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=252 uM for 4-CDP-2-C-methyl-D-erythritol 2-phosphate (at pH 7 and
CC in presence of Mg(2+) with recombinant IspF residues (62-240))
CC {ECO:0000269|PubMed:11389720};
CC Vmax=4.3 umol/min/mg enzyme (at pH 7 and in presence of Mg(2+) with
CC recombinant IspF residues (62-240)) {ECO:0000269|PubMed:11389720};
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:0000305|PubMed:11389720}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P62368}.
CC -!- SUBCELLULAR LOCATION: Plastid, apicoplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000305}.
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DR EMBL; AF279661; AAG09818.1; -; mRNA.
DR EMBL; CH671929; KOB59060.1; -; Genomic_DNA.
DR AlphaFoldDB; P62369; -.
DR SMR; P62369; -.
DR EnsemblProtists; KOB59060; KOB59060; PFHG_00813.
DR VEuPathDB; PlasmoDB:PfHB3_020014000; -.
DR BRENDA; 4.6.1.12; 4889.
DR SABIO-RK; P62369; -.
DR UniPathway; UPA00056; UER00095.
DR Proteomes; UP000054289; Unassembled WGS sequence.
DR GO; GO:0020011; C:apicoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-EC.
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:InterPro.
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 1: Evidence at protein level;
KW Apicoplast; Isoprene biosynthesis; Lyase; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Apicoplast"
FT /evidence="ECO:0000305"
FT CHAIN ?..240
FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT synthase, apicoplast"
FT /id="PRO_0000016485"
FT BINDING 71..73
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 71
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62368"
FT BINDING 73
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62368"
FT BINDING 115..116
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 123
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62368"
FT BINDING 137..139
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62368"
FT BINDING 142..146
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 181..187
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62368"
FT BINDING 212..214
FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate"
FT /ligand_id="ChEBI:CHEBI:57919"
FT /evidence="ECO:0000250|UniProtKB:P62368"
FT SITE 115
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT SITE 214
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62617"
SQ SEQUENCE 240 AA; 27161 MW; 7C46116F48B33D15 CRC64;
MFLKGYTSNV VLIILTFFIL LTKEEKNIKN NISGYCFLNF GLKKNAIIKK REKQNLKLFC
YNGIRIGQGY DIHKIKVLDE EYNTYANNDF NKNEQSFKTL TLGGVKINNV LVLSHSDGDI
IYHSIVDSIL GALGSLDIGT LFPDKDEKNK NKNSAIFLRY ARLLIYKKNY DIGNVDINVI
AQVPKISNIR KNIIKNISTV LNIDESQISV KGKTHEKLGV IGEKKAIECF ANILLIPKNS
