ID   ISPDF_RHOFD             Reviewed;         418 AA.
AC   Q21YT7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-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=Rfer_1332;
OS   Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
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., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM
RT   15236.";
RL   Submitted (FEB-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; CP000267; ABD69066.1; -; Genomic_DNA.
DR   RefSeq; YP_522597.1; -.
DR   GeneID; 3961363; -.
DR   GenomeReviews; CP000267_GR; Rfer_1332.
DR   KEGG; rfr:Rfer_1332; -.
DR   NMPDR; fig|338969.3.peg.2261; -.
DR   HOGENOM; Q21YT7; -.
DR   OMA; Q21YT7; IVLIHDA.
DR   BioCyc; RFER338969:RFER_1332-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    418       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000296752.
FT   REGION        1    261       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      262    418       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       268    268       Divalent metal cation (By similarity).
FT   METAL       270    270       Divalent metal cation (By similarity).
FT   METAL       302    302       Divalent metal cation (By similarity).
FT   SITE         29     29       Transition state stabilizer (By
FT                                similarity).
FT   SITE         36     36       Transition state stabilizer (By
FT                                similarity).
FT   SITE        169    169       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        222    222       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        294    294       Transition state stabilizer (By
FT                                similarity).
FT   SITE        393    393       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   418 AA;  44282 MW;  D172268F7456D43F CRC64;
     MADTPALIPQ SDTTPRCWAL IPCAGTGSRA GATGPKQYQL LAGKPMVLHT LAAFAAVPRI
     ARTLVVVAPD DAFFASQTLT DARFLVAACG GSTRAASVLN GLNFLLGQGA ARHDWVLVHD
     AARCLIRPDQ IDQLIDACWQ DDVGGLLALP LPDTLKRESL GRVAATLERA DKWLAQTPQM
     FRLGSLLDAL QVAGTTVTDE SSAMEAMGLS PKLVPGSAQN FKVTYPQDFC LAEAVLMTRS
     SGDSAPQQSA SEFKRASDMN FRIGEGWDIH ALVAGRKLLL GGVEIPYHLG LLGHSDADVL
     LHAITDALLG AAALGDIGTH FPDTDARFKG ADSLVLLTEA ARRVRAKGFE IGNVDSTVIA
     QAPKLMPYMA AMRAQIALAL ALEVDQVNVK AKTAEKMGPV GLGQAMEARA TVLLRKFI
//