ID   ISPDF_MARMM             Reviewed;         383 AA.
AC   Q0APQ6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=Mmar10_1439;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-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; CP000449; ABI65731.1; -; Genomic_DNA.
DR   RefSeq; YP_756669.1; -.
DR   GeneID; 4285678; -.
DR   GenomeReviews; CP000449_GR; Mmar10_1439.
DR   KEGG; mmr:Mmar10_1439; -.
DR   NMPDR; fig|394221.5.peg.1404; -.
DR   HOGENOM; Q0APQ6; -.
DR   OMA; Q0APQ6; 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   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    383       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000296749.
FT   REGION        1    226       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      227    383       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       233    233       Divalent metal cation (By similarity).
FT   METAL       235    235       Divalent metal cation (By similarity).
FT   METAL       267    267       Divalent metal cation (By similarity).
FT   SITE         15     15       Transition state stabilizer (By
FT                                similarity).
FT   SITE         22     22       Transition state stabilizer (By
FT                                similarity).
FT   SITE        152    152       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        206    206       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        259    259       Transition state stabilizer (By
FT                                similarity).
FT   SITE        358    358       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   383 AA;  40316 MW;  F5F0A75DABC804D4 CRC64;
     MKIAAVIVAA GRGERAGGGV PKQYRRLGGF FVLTHTLLRL LHREVFDSII VVVNPADADH
     IAAVEAELDI KLDTVPGGAT RTASVRAGLE RARDLGLDAV MIHDAARPFL GDALIDRLVK
     ALADHPAVIP ALPVADALFR GGDARMGDPV SRDGLYAAQT PQAFHLAPLL KAYARLGDTA
     LPDDAAVIRA AGGEVALVPG EAENFKLTTR ADFERAERQI MSETITVTGQ GYDVHRLEPA
     DVMWLCGVEI RAGLGLIGHS DADAGLHALT DAVLGAAGAG DIGQHFPPSD PQWKGAASDA
     FLLHAIKLLK QVGGELVHAD ITLIAERPKI GPHRDAMRAR VAELTGLPEK RVNIAATTTE
     KLGFTGRGEG LAAQAIVTAR LTT
//