ID   ISPDF_RHOCA             Reviewed;         379 AA.
AC   Q08113;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   05-MAY-2009, entry version 56.
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;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis;
RX   MEDLINE=93360820; PubMed=8355615;
RX   DOI=10.1111/j.1365-2958.1993.tb01636.x;
RA   Foster-Hartnett D., Cullen P.J., Gabbert K.K., Kranz R.G.;
RT   "Sequence, genetic, and lacZ fusion analyses of a nifR3-ntrB-ntrC
RT   operon in Rhodobacter capsulatus.";
RL   Mol. Microbiol. 8:903-914(1993).
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; X72382; CAA51072.1; -; Genomic_DNA.
DR   PIR; S34980; S34980.
DR   HSSP; P44815; 1JN1.
DR   BRENDA; 2.7.7.60; 567.
DR   BRENDA; 4.6.1.12; 567.
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   Isoprene biosynthesis; Lyase; Metal-binding; Multifunctional enzyme;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN         1    379       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000075675.
FT   REGION        1    223       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      224    379       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       230    230       Divalent metal cation (By similarity).
FT   METAL       232    232       Divalent metal cation (By similarity).
FT   METAL       264    264       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        146    146       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        199    199       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        256    256       Transition state stabilizer (By
FT                                similarity).
FT   SITE        355    355       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   379 AA;  39511 MW;  4A1A4377FBC34628 CRC64;
     MTVAVIIVAA GRGTRAGEGL PKQWRDLAGR PVLAQTVAAF AGLGRILVVL HPDDMGLGMD
     LLGGSVVLVA GGSTRSESVK NALEALEGSD VTRVLIHDGA RPLVPASVTA AVLAALETTP
     GAAPALAVTD ALWRGEAGLV AGTQDREGLY RAQTPQGFRF PEILAAHRAH PGGAADDVEV
     ARHAGLSVAI VPGHEDNLKI TYAPDFARAE AILRERKGLT MDVRLGNGYD VHAFCEGDHV
     VLCGVKVPHV KALLGHSDAD VGMHALTDAI YGALAEGDIG RHFPPSDPQW KGAASWIFLD
     HAAKLAKSRG FRIGNADVTL ICERPKVGPH AVAMAAELAR IMEIEPSRVS VKATTSERLG
     FTGREEGIAS IATVTLIGA
//