ID   ISPDF_RHOP2             Reviewed;         401 AA.
AC   Q2IW23;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=RPB_2885;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-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; CP000250; ABD07587.1; -; Genomic_DNA.
DR   RefSeq; YP_486498.1; -.
DR   GeneID; 3910679; -.
DR   GenomeReviews; CP000250_GR; RPB_2885.
DR   KEGG; rpb:RPB_2885; -.
DR   HOGENOM; Q2IW23; -.
DR   OMA; Q2IW23; IVLIHDA.
DR   BioCyc; RPAL316058:RPB_2885-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    401       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000296756.
FT   REGION        1    234       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      235    401       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   401 AA;  42361 MW;  51DF150C2A2EBF9C CRC64;
     MQKPPRTAAI IVAAGRGLRA GAGGPKQYRT LAGRPVIARA LQPFCTHPEV FAVQPVTNPD
     DTATFNEAVA GLDFRPAVGG GATRQASVRA GLEALAELNP DIVLIHDAAR PFVTPDLISR
     AIVAAGQTGA ALPVIAVNDT VKQVDAEGCV VATPDRAQLR IAQTPQAFRF DVILDAHRRA
     ARDGRDDFTD DAAIAEWAGL TVSTFEGDAA NMKLTTPEDF SREESRLTAA LGDIRTGTGY
     DVHAFGDGDH VWLCGLKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPTDPQ
     WKGAASDKFL KYAVDRVAAR GGRIANLEVT MICERPKIGP LRDPMRQRIA EITGVPVSRV
     AVKATTSERL GFTGREEGIA ATASATIRLP WSPWGAEGQA S
//