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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_HYPNA             Reviewed;         378 AA.
Q0C0N0;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
25-OCT-2017, entry version 75.
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=HNE_2014;
Hyphomonas neptunium (strain ATCC 15444).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Hyphomonadaceae; Hyphomonas.
NCBI_TaxID=228405;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15444;
PubMed=16980487; DOI=10.1128/JB.00111-06;
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
"Comparative genomic evidence for a close relationship between the
dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
crescentus.";
J. Bacteriol. 188:6841-6850(2006).
-!- 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; CP000158; ABI76497.1; -; Genomic_DNA.
RefSeq; WP_011647013.1; NC_008358.1.
ProteinModelPortal; Q0C0N0; -.
SMR; Q0C0N0; -.
STRING; 228405.HNE_2014; -.
EnsemblBacteria; ABI76497; ABI76497; HNE_2014.
KEGG; hne:HNE_2014; -.
eggNOG; ENOG4108UH8; Bacteria.
eggNOG; COG0245; LUCA.
eggNOG; COG1211; LUCA.
HOGENOM; HOG000252034; -.
KO; K12506; -.
OMA; GGDIGEW; -.
OrthoDB; POG091H023X; -.
UniPathway; UPA00056; UER00093.
UniPathway; UPA00056; UER00095.
Proteomes; UP000001959; Chromosome.
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; IPR001228; IspD.
InterPro; IPR026596; IspD/F.
InterPro; IPR034683; IspD/TarI.
InterPro; IPR018294; ISPD_synthase_CS.
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.
TIGRFAMs; TIGR00453; ispD; 1.
TIGRFAMs; TIGR00151; ispF; 1.
PROSITE; PS01295; ISPD; 1.
PROSITE; PS01350; ISPF; 1.
3: Inferred from homology;
Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding;
Multifunctional enzyme; Nucleotidyltransferase; Reference proteome;
Transferase.
CHAIN 1 378 Bifunctional enzyme IspD/IspF.
/FTId=PRO_0000292852.
REGION 1 222 2-C-methyl-D-erythritol 4-phosphate
cytidylyltransferase.
REGION 222 378 2-C-methyl-D-erythritol 2,4-
cyclodiphosphate synthase.
REGION 228 230 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
REGION 254 255 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
REGION 258 266 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
REGION 276 278 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
REGION 351 355 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01520}.
METAL 228 228 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_01520}.
METAL 230 230 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_01520}.
METAL 262 262 Divalent metal cation.
{ECO:0000255|HAMAP-Rule:MF_01520}.
BINDING 285 285 Substrate; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01520}.
BINDING 359 359 Substrate; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01520}.
BINDING 362 362 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01520}.
SITE 16 16 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
SITE 23 23 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
SITE 148 148 Positions MEP for the nucleophilic
attack. {ECO:0000255|HAMAP-
Rule:MF_01520}.
SITE 201 201 Positions MEP for the nucleophilic
attack. {ECO:0000255|HAMAP-
Rule:MF_01520}.
SITE 254 254 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
SITE 353 353 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01520}.
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


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