ID   ISPDF_ERYLH             Reviewed;         386 AA.
AC   Q2NAE1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-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=ELI_06290;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H.,
RA   Friedman R., Venter J.C.;
RL   Submitted (SEP-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; CP000157; ABC63350.1; -; Genomic_DNA.
DR   RefSeq; YP_458147.1; -.
DR   GeneID; 3871177; -.
DR   GenomeReviews; CP000157_GR; ELI_06290.
DR   KEGG; eli:ELI_06290; -.
DR   NMPDR; fig|314225.3.peg.1798; -.
DR   OMA; Q2NAE1; IVLIHDA.
DR   BioCyc; ELIT314225:ELI_06290-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    386       Bifunctional enzyme ispD/ispF.
FT                                /FTId=PRO_0000292851.
FT   REGION        1    226       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase.
FT   REGION      227    386       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT   METAL       233    233       Divalent metal cation (By similarity).
FT   METAL       235    235       Divalent metal cation (By similarity).
FT   METAL       267    267       Divalent metal cation (By similarity).
FT   SITE         22     22       Transition state stabilizer (By
FT                                similarity).
FT   SITE         29     29       Transition state stabilizer (By
FT                                similarity).
FT   SITE        157    157       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        212    212       Positions MEP for the nucleophilic attack
FT                                (By similarity).
FT   SITE        259    259       Transition state stabilizer (By
FT                                similarity).
FT   SITE        358    358       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   386 AA;  40308 MW;  41D3E50441D1CE2E CRC64;
     MATPSPLPSF AAIVVAAGKG LRAGQPVPKQ FATWRGKPVL RHSVESLRAA GADPIVVAIP
     DHAGDVAAKA LDGITEVVFV TGGQTRQDSV RAALERLSSV PPERVLIHDA ARAILPTPVI
     ERVLHGLDES GGAIPVLPVV DSLAVAAGER MADKADRESL RRVQTPQGFR FSDILAAHRA
     WTGATDAGDD AQVLMAHGGD IALVEGDEAL KKLTFAEDFM ADLLPVRVGT GFDVHKLEAG
     EELWLGGIRL EHDKGLAGHS DADVALHAIV DALLGAIGKG DIGDHFPPSD PQWKGAASSA
     FIEHAAKLVD EAGYRVGNID LTIICEAPRI GPHRDAMGQR IAELLATSPD AISVKATTTE
     KLGFTGRGEG IAAQAAATVV RKDTPA
//