ID   ISPDF_RHORT             Reviewed;         384 AA.
AC   Q2RTS1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-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=Rru_A1674;
OS   Rhodospirillum rubrum (strain ATCC 11170 / NCIB 8255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
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., Munk A.C., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G.,
RA   Reslewic S., Zhou S., Schwartz D.C.;
RT   "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC
RT   11170.";
RL   Submitted (DEC-2005) 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; CP000230; ABC22474.1; -; Genomic_DNA.
DR   RefSeq; YP_426761.1; -.
DR   GeneID; 3835094; -.
DR   GenomeReviews; CP000230_GR; Rru_A1674.
DR   KEGG; rru:Rru_A1674; -.
DR   NMPDR; fig|1085.1.peg.2251; -.
DR   HOGENOM; Q2RTS1; -.
DR   OMA; Q2RTS1; IVLIHDA.
DR   BioCyc; RRUB269796:RRU_A1674-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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding;
KW   Multifunctional enzyme; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    384       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000292860.
FT   REGION        1    227       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      228    384       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       234    234       Divalent metal cation (By similarity).
FT   METAL       236    236       Divalent metal cation (By similarity).
FT   METAL       268    268       Divalent metal cation (By similarity).
FT   SITE         16     16       Transition state stabilizer (By
FT                                similarity).
FT   SITE         23     23       Transition state stabilizer (By
FT                                similarity).
FT   SITE        153    153       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        207    207       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        260    260       Transition state stabilizer (By
FT                                similarity).
FT   SITE        359    359       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   384 AA;  40287 MW;  C50CD5FA4F5EF47C CRC64;
     MAKVAALIVA AGRGKRFGGD LPKQYQTLGG RPILRHTLAR FAAHPDVALV RAIIHPEDRD
     LYGAAAHGLA TLLDAVEGGA ERQDSVRLGL ESLTDVAPDY VLIHDGARPL VDGALIDRVI
     AALADHPGAI PALAVADTLK RGAGGMIGQT VDRAGLWRAQ TPQGFRYDAI LAAHRAQAGT
     MLTDDAAVLE AAGGAVALVD GAEDNAKITT FADLERAERL FRGEGEQRIG SGFDVHRLGP
     GDFVTLNGIR IPHSHGLVGH SDADAPMHAL TDALLGCLNA GDIGRHFPPS DMRWKGADSA
     IFLRHAAALI TALGGRILNV DITILCEQPK IGPHRARMSA RLAEILEISA TRVAVKATTT
     EELGFTGRGE GIAAQATALI TLPF
//