ISPF_CATRO
ID ISPF_CATRO Reviewed; 236 AA.
AC Q9M4W3;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, chloroplastic {ECO:0000305};
DE Short=MECDP-synthase {ECO:0000305};
DE Short=MECPS {ECO:0000305};
DE EC=4.6.1.12 {ECO:0000250|UniProtKB:Q9CAK8};
DE Flags: Precursor;
GN Name=ISPF; Synonyms=MECS;
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11118631; DOI=10.1016/s0167-4781(00)00240-2;
RA Veau B., Courtois M., Oudin A., Chenieux J.-C., Rideau M., Clastre M.;
RT "Cloning and expression of cDNAs encoding two enzymes of the MEP pathway in
RT Catharanthus roseus.";
RL Biochim. Biophys. Acta 1517:159-163(2000).
CC -!- FUNCTION: Converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-
CC phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP.
CC {ECO:0000250|UniProtKB:Q9CAK8}.
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:0000250|UniProtKB:Q9CAK8};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q9CAK8};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:Q9CAK8};
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}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q9CAK8}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q9CAK8}.
CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000305}.
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DR EMBL; AF250236; AAF65155.1; -; mRNA.
DR AlphaFoldDB; Q9M4W3; -.
DR SMR; Q9M4W3; -.
DR UniPathway; UPA00056; UER00095.
DR GO; GO:0009570; C:chloroplast stroma; 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 2: Evidence at transcript level;
KW Chloroplast; Isoprene biosynthesis; Lyase; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..236
FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT synthase, chloroplastic"
FT /id="PRO_0000016483"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 87
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 89
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 117..125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 121
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 135..137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 140..144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 179..185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT BINDING 210..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT SITE 113
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62617"
FT SITE 212
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P62617"
SQ SEQUENCE 236 AA; 25364 MW; 5AA0B0C8DB08AF03 CRC64;
MAMATSFYCS TAIPSKKTNQ NRENFLCSPV GGSKTTPSYI RLSTRQSRTL SLVVSAAASG
AAVEAEPKFA AVTPSKILSF RVGHGFDLHR LEPGYPLIIG GINIPHDRGC EAHSDGDVLL
HCVVDAILGA LGLPDIGQIF PDTDPKWKGA PSSVFIKEAV RLMDEAGYEL GNLDATLILQ
RPKVSPHKEA IRQNLCQLLG ADPCVVNLKA KTHEKVDSLG ENRSIAAHTV VLLMRK
