ID   ISPDF_NOVAD             Reviewed;         386 AA.
AC   Q2G708;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-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=Saro_1925;
OS   Novosphingobium aromaticivorans (strain DSM 12444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
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., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
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; CP000248; ABD26365.1; -; Genomic_DNA.
DR   RefSeq; YP_497199.1; -.
DR   GeneID; 3917148; -.
DR   GenomeReviews; CP000248_GR; Saro_1925.
DR   KEGG; nar:Saro_1925; -.
DR   NMPDR; fig|48935.1.peg.896; -.
DR   HOGENOM; Q2G708; -.
DR   OMA; Q2G708; IVLIHDA.
DR   BioCyc; NARO279238:SARO_1925-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   Gene3D; G3DSA:3.30.1330.50; MECDP_synthase_core; 1.
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    386       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000292857.
FT   REGION        1    230       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      231    386       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       237    237       Divalent metal cation (By similarity).
FT   METAL       239    239       Divalent metal cation (By similarity).
FT   METAL       271    271       Divalent metal cation (By similarity).
FT   SITE         24     24       Transition state stabilizer (By
FT                                similarity).
FT   SITE         31     31       Transition state stabilizer (By
FT                                similarity).
FT   SITE        159    159       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        214    214       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        263    263       Transition state stabilizer (By
FT                                similarity).
FT   SITE        362    362       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   386 AA;  40153 MW;  716C422DEB3B7D17 CRC64;
     MNSVPSLPGQ SVAAVVVAGG KGLRTGGPVP KQFVIWRGKP LLRHCVEALE AAGIAPIVVA
     IPAGWDEAAT QALAGISMVR LVHGGATRQE SVKAALEVLE GDAPARVLIH DAARPDLPGS
     VIERLLTALD KRTGAIPVLP VVDSMVRGSG DAMGETVARE DLYRVQTPQA FHYPAILAAH
     RAWQGEALAG DDAQVAMRAA HEIALVEGDE ALRKVTFASD LEEQSMSVIP RTGMGFDVHR
     LVEGEELWLC GVNIPHGKGL SGHSDADVAI HALVDALLGA IAAGDIGDHF PPSDPQWKGA
     SSDRFLAHAG TLVTEAGYRI ANVDVTIICE APKIGPHKAA MRETLARILG IDSALVSVKA
     TTTERLGLTG RGEGIAAQAV ATVVSG
//