ID   ISPDF_RHIL3             Reviewed;         405 AA.
AC   Q1MH21;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-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=RL2254;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R.,
RA   Ghazoui Z.F., Hull K.H., Wexler M., Curson A.R.J., Todd J.D.,
RA   Poole P.S., Mauchline T.H., East A.K., Quail M.A., Churcher C.,
RA   Arrowsmith C., Cherevach I., Chillingworth T., Clarke K., Cronin A.,
RA   Davis P., Fraser A., Hance Z., Hauser H., Jagels K., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and
RT   accessory components.";
RL   Genome Biol. 7:RESEARCH34.1-RESEARCH34.20(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; AM236080; CAK07746.1; -; Genomic_DNA.
DR   RefSeq; YP_767848.1; -.
DR   GeneID; 4402763; -.
DR   GenomeReviews; AM236080_GR; RL2254.
DR   KEGG; rle:RL2254; -.
DR   NMPDR; fig|216596.1.peg.2335; -.
DR   HOGENOM; Q1MH21; -.
DR   OMA; Q1MH21; IVLIHDA.
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    405       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000296751.
FT   REGION        1    246       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      247    405       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       253    253       Divalent metal cation (By similarity).
FT   METAL       255    255       Divalent metal cation (By similarity).
FT   METAL       287    287       Divalent metal cation (By similarity).
FT   SITE         24     24       Transition state stabilizer (By
FT                                similarity).
FT   SITE         33     33       Transition state stabilizer (By
FT                                similarity).
FT   SITE        167    167       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        224    224       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        279    279       Transition state stabilizer (By
FT                                similarity).
FT   SITE        378    378       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   405 AA;  43345 MW;  166CBA488D008CAD CRC64;
     MLQMPSKQPI SAGIVIVAAG RGERAGSSKE GPKQYRMIGG KPVIVHTLEN FMTWEAATEI
     VVVIHPDDEA LFARAFRHII SATPIETVHG GATRQQSVLA GLRYLKDKQI SHVLIHDAVR
     PFFDHALLDR IAESLDAGAQ AVLPAIPVTD TLKRADNAGT VLTTVSREHL YAAQTPQSFA
     FETILEAHEK AAASGRSDFT DDASIAEWLG IPVTIVEGTA DNVKLTVKDD IAMADDKLSA
     SLLPDVRTGN GYDVHQLVAG DGVTLCGVFI PHDQKLKGHS DADVALHALT DALLATCGAG
     DIGDHFPPSD PQWKGAASRI FIEHAARIVR ERGGTIMNAD VSLIAEAPKV GPHRDAMRAK
     LSDYLGIDIE RCSVKATTNE TIGFVGRREG IAAIATATVV YRGRK
//