ID   ISPDF_GRABC             Reviewed;         376 AA.
AC   Q0BTD5;
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=GbCGDNIH1_1019;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17827295; DOI=10.1128/JB.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K.,
RA   Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W.,
RA   Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61917.1; -; Genomic_DNA.
DR   RefSeq; YP_744840.1; -.
DR   GeneID; 4275844; -.
DR   GenomeReviews; CP000394_GR; GbCGDNIH1_1019.
DR   KEGG; gbe:GbCGDNIH1_1019; -.
DR   NMPDR; fig|391165.8.peg.1020; -.
DR   HOGENOM; Q0BTD5; -.
DR   OMA; Q0BTD5; 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    376       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000296745.
FT   REGION        1    219       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      220    376       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       226    226       Divalent metal cation (By similarity).
FT   METAL       228    228       Divalent metal cation (By similarity).
FT   METAL       260    260       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        252    252       Transition state stabilizer (By
FT                                similarity).
FT   SITE        351    351       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   376 AA;  39766 MW;  40820CD0A8BE074F CRC64;
     MRIAAILVAG GSGSRFGSDI PKQFLPVGGK PLIRHGAERL SAKVDLLQPV GCADDIAPLL
     QGLDHLPIVD GGKERQDSVR AGLEALVPYA PDIVLIHDAA RPYFPDHTIE DLIEALQIHD
     GAIPAVPVAD TLKRAAGNII DSTVPREGLY RAQTPQAFKF SVLLALHRDH PGGATDDAAL
     LDQAGHSVAL VPGAEDNIKV TYPADLARVE RSMSISMIPR IGTGYDVHAF ETGRKLILCG
     IEVPHHQGLA GHSDADVGIH ALCDAIYGAL AEGDIGRHFP PTEASWKDAD SARFLRHAAE
     RIAARGGFLA NADLTLICEK PKITPHAPAM IARLAELLGV SIDKISVKAT TSEKLGFTGR
     EEGIAAQAAV IIMIPA
//