ID   ISPDF_RHOPS             Reviewed;         398 AA.
AC   Q137C3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=RPD_2587;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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; CP000283; ABE39816.1; -; Genomic_DNA.
DR   RefSeq; YP_569717.1; -.
DR   GeneID; 4023083; -.
DR   GenomeReviews; CP000283_GR; RPD_2587.
DR   KEGG; rpd:RPD_2587; -.
DR   HOGENOM; Q137C3; -.
DR   OMA; Q137C3; IVLIHDA.
DR   BioCyc; RPAL316057:RPD_2587-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   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    398       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000296755.
FT   REGION        1    234       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      235    398       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       241    241       Divalent metal cation (By similarity).
FT   METAL       243    243       Divalent metal cation (By similarity).
FT   METAL       275    275       Divalent metal cation (By similarity).
FT   SITE         19     19       Transition state stabilizer (By
FT                                similarity).
FT   SITE         26     26       Transition state stabilizer (By
FT                                similarity).
FT   SITE        156    156       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        213    213       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        267    267       Transition state stabilizer (By
FT                                similarity).
FT   SITE        366    366       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   398 AA;  42012 MW;  041CE38B0B57B9C9 CRC64;
     MPNPPRTAAI IVAAGRGLRA GAGGPKQYRT LAGRPVIARA LQPFCTHPEV FAVQPVTNPD
     DTAIFNDAVT GLNFRPAVGG GATRQGSVRA GLEALAELNP DIVLIHDAAR PFVTPDLISR
     AIVAAGQTGA ALPVVAINDT VKQINAEGCV EATPDRARLR IAQTPQAFRF DVILDAHRRA
     ARDGRDDFTD DAAIAEWAGL TVSTFEGDAA NMKLTTPDDF IREESRLTAL LGDIRTGTGY
     DVHAFGDGDH VWLCGLKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPTDPQ
     WKGAASDKFL KYAVERVAAR GGRIANLEVT MICERPKIGP LREAMRARIA EITGLPVSRI
     AVKATTSERL GFTGREEGIA ATASATIRLP WGAEGLAG
//