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

 A0A074JTX8_9RHOB        Unreviewed;       375 AA.
A0A074JTX8;
01-OCT-2014, integrated into UniProtKB/TrEMBL.
01-OCT-2014, sequence version 1.
12-SEP-2018, entry version 36.
RecName: Full=Bifunctional enzyme IspD/IspF {ECO:0000256|HAMAP-Rule:MF_01520};
Includes:
RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01520};
Short=MECDP-synthase {ECO:0000256|HAMAP-Rule:MF_01520};
Short=MECPP-synthase {ECO:0000256|HAMAP-Rule:MF_01520};
Short=MECPS {ECO:0000256|HAMAP-Rule:MF_01520};
EC=4.6.1.12 {ECO:0000256|HAMAP-Rule:MF_01520};
Includes:
RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520};
EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_01520};
AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_01520};
AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520};
Short=MCT {ECO:0000256|HAMAP-Rule:MF_01520};
Name=ispDF {ECO:0000256|HAMAP-Rule:MF_01520};
ORFNames=DT23_04525 {ECO:0000313|EMBL:KEO59350.1};
Thioclava indica.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Thioclava.
NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO59350.1, ECO:0000313|Proteomes:UP000027471};
[1] {ECO:0000313|EMBL:KEO59350.1, ECO:0000313|Proteomes:UP000027471}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DT23-4 {ECO:0000313|EMBL:KEO59350.1,
ECO:0000313|Proteomes:UP000027471};
PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
"Thioclava indica sp. nov., isolated from surface seawater of the
Indian Ocean.";
Antonie Van Leeuwenhoek 107:297-304(2015).
-!- 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:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00771987}.
-!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C-
methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
+ CMP. {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00771955}.
-!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate =
diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol.
{ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|SAAS:SAAS00709147}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00771949};
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000256|HAMAP-
Rule:MF_01520, ECO:0000256|SAAS:SAAS00709253}.
-!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000256|HAMAP-
Rule:MF_01520, ECO:0000256|SAAS:SAAS00771963}.
-!- SIMILARITY: In the C-terminal section; belongs to the IspF family.
{ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|SAAS:SAAS00771954}.
-!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI
cytidylyltransferase family. IspD subfamily. {ECO:0000256|HAMAP-
Rule:MF_01520, ECO:0000256|SAAS:SAAS00771938}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01520}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEO59350.1}.
-----------------------------------------------------------------------
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EMBL; AUNB01000029; KEO59350.1; -; Genomic_DNA.
RefSeq; WP_038131049.1; NZ_AUNB01000029.1.
EnsemblBacteria; KEO59350; KEO59350; DT23_04525.
UniPathway; UPA00056; UER00093.
UniPathway; UPA00056; UER00095.
Proteomes; UP000027471; Unassembled WGS sequence.
GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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_00108; IspD; 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 {ECO:0000313|Proteomes:UP000027471};
Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00771928};
Lyase {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00771989};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00771962};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00771957};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00981526};
Reference proteome {ECO:0000313|Proteomes:UP000027471};
Transferase {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00981526}.
DOMAIN 219 372 YgbB. {ECO:0000259|Pfam:PF02542}.
REGION 1 219 2-C-methyl-D-erythritol 4-phosphate
cytidylyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 220 375 2-C-methyl-D-erythritol 2,4-
cyclodiphosphate synthase.
{ECO:0000256|HAMAP-Rule:MF_01520}.
REGION 226 228 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 252 253 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 256 264 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 274 276 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 349 353 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
METAL 226 226 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01520}.
METAL 228 228 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01520}.
METAL 260 260 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01520}.
BINDING 283 283 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01520}.
BINDING 357 357 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01520}.
BINDING 360 360 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01520}.
SITE 15 15 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SITE 22 22 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SITE 146 146 Positions MEP for the nucleophilic
attack. {ECO:0000256|HAMAP-
Rule:MF_01520}.
SITE 199 199 Positions MEP for the nucleophilic
attack. {ECO:0000256|HAMAP-
Rule:MF_01520}.
SITE 252 252 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SITE 351 351 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SEQUENCE 375 AA; 39273 MW; 7C9728B925DD1A46 CRC64;
MDTAVIIVAA GRGTRAGGDA PKQWQLLAGQ PVLAHTVARF AGVGRIIVVL HPEDMARGVA
LFRGAVVLCA GGQTRDGSVR NALEMLEGSG VTRVLIHDGA RPLVSRAVIE GVLSALDTHR
AAAPALAVSD ALWIGSNGQV TGTQDRSNLW RAQTPQGFDF DTILAAHRTH PGGAADDVEV
VRAAGVDVAI TPGSEDNLKI TYPADFARAE RILGTKMDIR LGHGYDVHAF EDGDHVILCG
VRVPHSAALK GHSDADVGMH ALTDAIYGAL AEGDIGRHFP PSDPQWKGAA SEIFLDHAAK
LAEARGFRIG NVDVTLICEQ PKIGPHASAM AQELARIIGL EPGRISVKAT TSERLGFTGR
EEGIAAIATA TLIAE


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