ID   ISPDF_NITWN             Reviewed;         398 AA.
AC   Q3SSN8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Nwi_1442;
OS   Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L.,
RA   Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J.,
RA   Arp D.J., Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing
RT   bacterium Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA04703.1; -; Genomic_DNA.
DR   RefSeq; YP_318055.1; -.
DR   GeneID; 3677184; -.
DR   GenomeReviews; CP000115_GR; Nwi_1442.
DR   KEGG; nwi:Nwi_1442; -.
DR   NMPDR; fig|323098.3.peg.1517; -.
DR   HOGENOM; Q3SSN8; -.
DR   OMA; Q3SSN8; IVLIHDA.
DR   BioCyc; NWIN323098:NWI_1442-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_0000296750.
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;  42115 MW;  2A51DA2EB5BC0930 CRC64;
     MPSSKRTAAI IVAAGRGLRA GAGGPKQYRT IGGRTVISRA MEAFCQHPDV FAVQPVLNPD
     DLSMFNQAAA QFRYRPPANG GATRQASVRA GLEALAADAP DIVLIHDAAR PFVTPALITR
     AIDAADKAGA AVPAIAVTDT IKQVDESGAV NATPDRAKLR IAQTPQAFHF DMILDAHRRA
     AREGRDDFTD DAALAEWVGL TVATFEGDAA NMKLTTPEDF VREEARLAAA LGDIRTGTGY
     DVHAFGEGDH LMLCGVKVPH NCGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDPQ
     WKGAASDKFL KYAVDRVTAR GGRVANLEVT MICQQPKIGP LRDQMRARIA DITGVAISRI
     AVKATTSERL GFTGREEGIA ATASATIRLP WNDKGRDT
//