ID   ISPDF_MESSB             Reviewed;         408 AA.
AC   Q11HV9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Bifunctional enzyme ispD/ispF;
DE   Includes:
DE     RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase;
DE              EC=2.7.7.60;
DE     AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase;
DE     AltName: Full=MEP cytidylyltransferase;
DE              Short=MCT;
DE   Includes:
DE     RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase;
DE              Short=MECPS;
DE              Short=MECDP-synthase;
DE              EC=4.6.1.12;
GN   Name=ispDF; OrderedLocusNames=Meso_1621;
OS   Mesorhizobium sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the formation of 4-
CC       diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-
CC       D-erythritol 4-phosphate (MEP) (ispD), and converts 4-
CC       diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-
CC       methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP (ispF)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate =
CC       diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C-
CC       methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
CC       + CMP.
CC   -!- COFACTOR: Divalent metal cations (By similarity).
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via
CC       DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate:
CC       step 2/6.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via
CC       DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate:
CC       step 4/6.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ispD family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ispF family.
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DR   EMBL; CP000390; ABG63016.1; -; Genomic_DNA.
DR   RefSeq; YP_674181.1; -.
DR   GeneID; 4179827; -.
DR   GenomeReviews; CP000390_GR; Meso_1621.
DR   KEGG; mes:Meso_1621; -.
DR   NMPDR; fig|266779.1.peg.367; -.
DR   HOGENOM; Q11HV9; -.
DR   OMA; Q11HV9; IVLIHDA.
DR   BioCyc; MSP266779:MESO_1621-MON; -.
DR   GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphat...; IEA:HAMAP.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidyl...; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01520; -; 1.
DR   InterPro; IPR001228; ISPD_synthase.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR003526; MECDP_synthase_core.
DR   Gene3D; G3DSA:3.30.1330.50; MECDP_synthase_core; 1.
DR   Pfam; PF01128; IspD; 1.
DR   Pfam; PF02542; YgbB; 1.
DR   TIGRFAMs; TIGR00453; ispD; 1.
DR   TIGRFAMs; TIGR00151; ispF; 1.
DR   PROSITE; PS01295; ISPD; 1.
DR   PROSITE; PS01350; ISPF; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding;
KW   Multifunctional enzyme; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    408       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000292855.
FT   REGION        1    247       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      248    408       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       254    254       Divalent metal cation (By similarity).
FT   METAL       256    256       Divalent metal cation (By similarity).
FT   METAL       288    288       Divalent metal cation (By similarity).
FT   SITE         26     26       Transition state stabilizer (By
FT                                similarity).
FT   SITE         35     35       Transition state stabilizer (By
FT                                similarity).
FT   SITE        166    166       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        223    223       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        280    280       Transition state stabilizer (By
FT                                similarity).
FT   SITE        379    379       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   408 AA;  43219 MW;  92FC006A88AAC43A CRC64;
     MNAPFEKDRR NRRVAVVVVA AGRGERAGQA QNGPKQYRLI GGKPVIRHTL EVLAKSKRVG
     TIAVAVHPED SSLFNQAREG LDGDIRAVHG GASRQESTRL ALAALEEVKP DIVLIHDGVR
     PFIDEALIER VIEAVGEDSG ALPALPVSDT LKRSGVNGII TGTVPRDGLF AAQTPQGFPF
     RPIYEAHQKA WQSGRSDFTD DAAIAEWAGI SVRLVSGSPD NVKLTWAKDI ALADQRLGPA
     MTELPDIRVG NGYDVHGFGP GGHVTLCGVQ IPHGKTLMGH SDADVGLHAL TDALLATCGA
     GDIGTHFPPS DPQWKGAKSR IFVEHAVNLL RARGGRIANA DVTLICEAPR IGPYREAMLA
     ELSDMLQISP ERVSVKATTN EGLGFIGRAE GIAAIATATV AYPGSLGN
//