ID   ISPDF_NITHX             Reviewed;         403 AA.
AC   Q1QM99;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   05-MAY-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=Nham_1834;
OS   Nitrobacter hamburgensis (strain X14 / DSM 10229).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323097;
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., Kyrpides N., Ivanova N., Ward B.,
RA   Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L.,
RA   Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
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; CP000319; ABE62648.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_577108.1; -.
DR   GeneID; 4033011; -.
DR   GenomeReviews; CP000319_GR; Nham_1834.
DR   KEGG; nha:Nham_1834; -.
DR   NMPDR; fig|323097.3.peg.3209; -.
DR   HOGENOM; Q1QM99; -.
DR   BioCyc; NHAM323097:NHAM_1834-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    403       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000292856.
FT   REGION        1    234       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      235    403       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   403 AA;  42798 MW;  C18698298DDC8335 CRC64;
     MPTSKRTAAI IVAAGRGLRA GTGGPKQYRT IAGRTVIARA MEAFCDHPDV FAVQPVLNPD
     DLAMFNQAVA GFRYRPPANG GATRQASVHA GLEALAADAP DIVLIHDAAR PFATPALIRR
     AIEATDITGA AVPVIPVTDT IKQVDASGAV NATPDRAKLR IAQTPQAFRF DVILDAHRRA
     ARDGRDDFTD DAALAEWVGL TVATFEGDAA NMKLTTPEDF VREEARLAAM LGDIRTGTGY
     DVHAFGDGDH VMLCGVKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDPQ
     WKGAASDKFL KYAVDRVAAR GGRIANLEVT MICERPKIGP LRDTMRARIA EITGVAISRI
     AVKATTSERL GFTGREEGIA TTASATVRLP WNDSDQEDKG WST
//