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Bifunctional enzyme IspD/IspF [Includes: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) (MEP cytidylyltransferase) (MCT); 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MECDP-synthase) (MECPP-synthase) (MECPS) (EC 4.6.1.12)]

 ISPDF_TROW8             Reviewed;         422 AA.
Q83NK3;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 89.
RecName: Full=Bifunctional enzyme IspD/IspF {ECO:0000255|HAMAP-Rule:MF_01520};
Includes:
RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_01520};
EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_01520};
AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_01520};
AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_01520};
Short=MCT {ECO:0000255|HAMAP-Rule:MF_01520};
Includes:
RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01520};
Short=MECDP-synthase {ECO:0000255|HAMAP-Rule:MF_01520};
Short=MECPP-synthase {ECO:0000255|HAMAP-Rule:MF_01520};
Short=MECPS {ECO:0000255|HAMAP-Rule:MF_01520};
EC=4.6.1.12 {ECO:0000255|HAMAP-Rule:MF_01520};
Name=ispDF {ECO:0000255|HAMAP-Rule:MF_01520}; OrderedLocusNames=TW422;
Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
Bacteria; Actinobacteria; Micrococcales; Tropheryma.
NCBI_TaxID=218496;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TW08/27;
PubMed=12606174; DOI=10.1016/S0140-6736(03)12597-4;
Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A.,
Dover L.G., Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E.,
von Herbay A., Goble A., Rutter S., Squares R., Squares S.,
Barrell B.G., Parkhill J., Relman D.A.;
"Sequencing and analysis of the genome of the Whipple's disease
bacterium Tropheryma whipplei.";
Lancet 361:637-644(2003).
-!- FUNCTION: Bifunctional enzyme that catalyzes the formation of 4-
diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-
D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the
conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-
phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-
cyclodiphosphate (ME-CPP) with a corresponding release of cytidine
5-monophosphate (CMP) (IspF). {ECO:0000255|HAMAP-Rule:MF_01520}.
-!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate =
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
{ECO:0000255|HAMAP-Rule:MF_01520}.
-!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C-
methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
+ CMP. {ECO:0000255|HAMAP-Rule:MF_01520}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000255|HAMAP-Rule:MF_01520};
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000255|HAMAP-
Rule:MF_01520}.
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000255|HAMAP-
Rule:MF_01520}.
-!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI
cytidylyltransferase family. IspD subfamily. {ECO:0000255|HAMAP-
Rule:MF_01520}.
-!- SIMILARITY: In the C-terminal section; belongs to the IspF family.
{ECO:0000255|HAMAP-Rule:MF_01520}.
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EMBL; BX251411; CAD67092.1; -; Genomic_DNA.
RefSeq; WP_011096372.1; NC_004551.1.
ProteinModelPortal; Q83NK3; -.
SMR; Q83NK3; -.
EnsemblBacteria; CAD67092; CAD67092; TW422.
GeneID; 29578259; -.
KEGG; tws:TW422; -.
HOGENOM; HOG000252034; -.
KO; K12506; -.
OMA; GGDIGEW; -.
OrthoDB; POG091H023X; -.
UniPathway; UPA00056; UER00093.
UniPathway; UPA00056; UER00095.
GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-EC.
GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
CDD; cd02516; CDP-ME_synthetase; 1.
CDD; cd00554; MECDP_synthase; 1.
Gene3D; 3.30.1330.50; -; 1.
Gene3D; 3.90.550.10; -; 1.
HAMAP; MF_01520; IspDF; 1.
HAMAP; MF_00107; IspF; 1.
InterPro; IPR026596; IspD/F.
InterPro; IPR034683; IspD/TarI.
InterPro; IPR003526; MECDP_synthase.
InterPro; IPR020555; MECDP_synthase_CS.
InterPro; IPR036571; MECDP_synthase_sf.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF01128; IspD; 1.
Pfam; PF02542; YgbB; 1.
SUPFAM; SSF53448; SSF53448; 1.
SUPFAM; SSF69765; SSF69765; 1.
PROSITE; PS01350; ISPF; 1.
3: Inferred from homology;
Isoprene biosynthesis; Lyase; Metal-binding; Multifunctional enzyme;
Nucleotidyltransferase; Transferase.
CHAIN 1 422 Bifunctional enzyme IspD/IspF.
/FTId=PRO_0000075679.
REGION 1 267 2-C-methyl-D-erythritol 4-phosphate
cytidylyltransferase.
REGION 268 422 2-C-methyl-D-erythritol 2,4-
cyclodiphosphate synthase.
REGION 274 276 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
REGION 301 302 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
REGION 323 325 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
METAL 274 274 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_01520}.
METAL 276 276 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_01520}.
METAL 309 309 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_01520}.
BINDING 404 404 Substrate; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01520}.
BINDING 407 407 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01520}.
SITE 15 15 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
SITE 22 22 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
SITE 170 170 Positions MEP for the nucleophilic
attack. {ECO:0000255|HAMAP-
Rule:MF_01520}.
SITE 226 226 Positions MEP for the nucleophilic
attack. {ECO:0000255|HAMAP-
Rule:MF_01520}.
SITE 301 301 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
SITE 398 398 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
SEQUENCE 422 AA; 45323 MW; 1ED382DBD6AC5EEC CRC64;
MAVGLLLLAA GVGSRLSSSL PKAFVSVGGL DLIQWCLKNL GQLRTALEVV VTVPKGFVEL
CERNVLQSLG TLEKIKIVTG GATRQDSVGL GIRYFSARIT KLLVHDVARA FTPPEIYLSV
IKQLETSKAV IPVIAIVDSI KKVNMQDAYR EVARGPGEPF HTKSVLHLDR REFFSAQTPQ
GFDRALLEAA HERSVASNEQ FADDSVMVAQ IEKDITLING HEASFKVTNP CDLQRAEFAA
SSLLSKSNVS PVNISQPPIS ALSMPLPLIG VGIDFHKFIL DESPLFLACL EWKNYRRLQG
HSDGDVVAHA CTTALLSAAN MGDIGSVFGV DLAATKDASG AYFLESTNRL LATNGFCVLN
IAVQVISNTP RLADRRVEAE HAISDCLSGA RISLSSVTTD GMGFLGRGEG IGAIAVAQIY
HR


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