ID   ISPDF_HYPNA             Reviewed;         378 AA.
AC   Q0C0N0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=HNE_2014;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
RA   Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
RA   Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
RA   Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
RA   Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
RA   Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(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; CP000158; ABI76497.1; -; Genomic_DNA.
DR   RefSeq; YP_760713.1; -.
DR   GeneID; 4287822; -.
DR   GenomeReviews; CP000158_GR; HNE_2014.
DR   KEGG; hne:HNE_2014; -.
DR   NMPDR; fig|228405.5.peg.1940; -.
DR   TIGR; HNE_2014; -.
DR   HOGENOM; Q0C0N0; -.
DR   OMA; Q0C0N0; IVLIHDA.
DR   BioCyc; HNEP81032:HNE_2014-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    378       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000292852.
FT   REGION        1    221       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      222    378       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       228    228       Divalent metal cation (By similarity).
FT   METAL       230    230       Divalent metal cation (By similarity).
FT   METAL       262    262       Divalent metal cation (By similarity).
FT   SITE         16     16       Transition state stabilizer (By
FT                                similarity).
FT   SITE         23     23       Transition state stabilizer (By
FT                                similarity).
FT   SITE        148    148       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        201    201       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        254    254       Transition state stabilizer (By
FT                                similarity).
FT   SITE        353    353       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   378 AA;  39494 MW;  B5AB6F7A04775D5F CRC64;
     MTETVAIIVA GGRGQRAGAE RPKQWQMLLG KRVIDWSIAA FVDHPQISQV VIVAGDELGD
     CSAEPKIIQA KPGNTRTQSV LSGLAAATIS EDATVVIHDA ARPGIDAATI SSLIARLQDP
     SVSGAAPAMP VADALKTNSG QSWTNVDRTG LVRVQTPQAF RLGEIRAALS AAGPDLVDDL
     TAIEAAGGRV EIVSGSARLT KITYPEDFDM LARLLSPTGA PRIGKGYDVH EFEAGDHVTL
     CGVAIPHIAK LKGHSDADAA WHALTDAILG AVALGDIGDH FPPSDPQWKG ADSGLFLKEA
     QRLAEAKGYV IANCDITVIC EAPKVKPHRE AMRARTAELL GLPLDAVSVK ATTTEGLGFT
     GRREGIAAEA VALLMPKG
//