ID   ISPDF_LAWIP             Reviewed;         399 AA.
AC   Q1MR76;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=LI0446;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the
RT   causative agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) 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; AM180252; CAJ54500.1; -; Genomic_DNA.
DR   RefSeq; YP_594822.1; -.
DR   GeneID; 4060193; -.
DR   GenomeReviews; AM180252_GR; LI0446.
DR   KEGG; lip:LI0446; -.
DR   HOGENOM; Q1MR76; -.
DR   OMA; Q1MR76; 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    399       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000296748.
FT   REGION        1    235       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      236    399       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       242    242       Divalent metal cation (By similarity).
FT   METAL       244    244       Divalent metal cation (By similarity).
FT   METAL       283    283       Divalent metal cation (By similarity).
FT   SITE         15     15       Transition state stabilizer (By
FT                                similarity).
FT   SITE         24     24       Transition state stabilizer (By
FT                                similarity).
FT   SITE        160    160       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        216    216       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        275    275       Transition state stabilizer (By
FT                                similarity).
FT   SITE        374    374       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   399 AA;  43819 MW;  5DA3E66FA1C0378C CRC64;
     METWALILAA GQGSRLLSTI GIAKQFFVWK GIPLYWQSVL QFMHCARIRG VVLVFPSEVK
     DNEEKVVDRL AAQYDLRLPY IVISGGKLRQ DSVKNALNTL PKNCSHVLIH DAARPFISPK
     LINNVIEVLE AGAVGVVPGI SVTDTIKQVI QGEVIVTRPR EQLIAVQTPQ GFHLKTIVEG
     HNRATLEKWT VTDDASLLEL CGHTVQVING EIENRKISFP QDLLYMVEQP KTTVPIVGYG
     YDVHKYVTED QINQPIRSMR LGGISIPNAP NVVAHSDGDV LLHALMDALL GCIGGGDIGL
     HFPDSDKRYD GINSAILLDH VLTKVLESSI KIVHMDATIV AQLPKISQYR EAIRSNLSRL
     LDLDLANVNI KATTEEGLGF TGECKGIKAI VIVTAIRIS
//