ID   ISPDF_PELUB             Reviewed;         371 AA.
AC   Q4FM31;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=SAR11_0945;
OS   Pelagibacter ubique.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   SAR11 cluster; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L.,
RA   Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M.,
RA   Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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; CP000084; AAZ21757.1; -; Genomic_DNA.
DR   RefSeq; YP_266361.1; -.
DR   GeneID; 3516956; -.
DR   GenomeReviews; CP000084_GR; SAR11_0945.
DR   KEGG; pub:SAR11_0945; -.
DR   HOGENOM; Q4FM31; -.
DR   OMA; Q4FM31; IVLIHDA.
DR   BioCyc; CPEL335992:SAR11_0945-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   Pfam; PF01128; IspD; 1.
DR   Pfam; PF02542; YgbB; 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    371       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000075672.
FT   REGION        1    214       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      215    371       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       221    221       Divalent metal cation (By similarity).
FT   METAL       223    223       Divalent metal cation (By similarity).
FT   METAL       255    255       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        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        247    247       Transition state stabilizer (By
FT                                similarity).
FT   SITE        346    346       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   371 AA;  41583 MW;  F2B8D25AB6985FC8 CRC64;
     MNSCFIILAG GESKRFNSNT PKPYTNYKGK PLLLHSIDKA KVFNKFNKIV LVVNKKHKNF
     IKKLNIKNIR IITGGKTRAE SAYNALKSIK ENNFKNVIIH DAARPNFSLK LLNKLMNELK
     LNDCVIPAIQ TADTVKQKIS NNVKNLKREN IYLIQTPQAF NYKKLFELQN NKSEEVTDDA
     NLFVRAGKKI KIIKGETTNN KITINSDIKF NNLIKFGIGF DVHRLVPNKK LYLGGVKIPS
     PIGTLGHSDG DPVLHAVTDA ILGACSMGDI GEKFSDKNKK FKNIRSTILL SEIIKQTLKK
     GYLINNLDIN IITQKPKIQK YKKQILNCIA KICNISPTQI NIKGKTTEKL GVIGKEKAIA
     CEVIASVIKN D
//