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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)]

 A0A0S4XP46_9PROT        Unreviewed;       372 AA.
A0A0S4XP46;
17-FEB-2016, integrated into UniProtKB/TrEMBL.
17-FEB-2016, sequence version 1.
22-NOV-2017, entry version 21.
RecName: Full=Bifunctional enzyme IspD/IspF {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=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520};
Short=MCT {ECO:0000256|HAMAP-Rule:MF_01520};
AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {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};
Name=ispDF {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000313|EMBL:CUV65854.1};
ORFNames=BN3087_480006 {ECO:0000313|EMBL:CUV65854.1};
Sulfurovum sp. enrichment culture clone C5.
Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum;
environmental samples.
NCBI_TaxID=497650 {ECO:0000313|EMBL:CUV65854.1};
[1] {ECO:0000313|EMBL:CUV65854.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN30871 {ECO:0000313|EMBL:CUV65854.1};
Zhang Y., Guo Z.;
Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
-!- 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|RuleBase:RU004395, 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:SAAS00771956}.
-!- 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:SAAS00771926}.
-!- 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: Belongs to the IspF family.
{ECO:0000256|RuleBase:RU004395}.
-!- 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}.
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EMBL; FAXN01000049; CUV65854.1; -; Genomic_DNA.
UniPathway; UPA00056; UER00093.
UniPathway; UPA00056; UER00095.
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_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.
TIGRFAMs; TIGR00151; ispF; 1.
PROSITE; PS01350; ISPF; 1.
3: Inferred from homology;
Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS00771928};
Lyase {ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|RuleBase:RU004395,
ECO:0000256|SAAS:SAAS00771989, ECO:0000313|EMBL:CUV65854.1};
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:SAAS00709227, ECO:0000313|EMBL:CUV65854.1};
Transferase {ECO:0000256|HAMAP-Rule:MF_01520,
ECO:0000256|SAAS:SAAS00709227, ECO:0000313|EMBL:CUV65854.1}.
DOMAIN 213 364 YgbB. {ECO:0000259|Pfam:PF02542}.
REGION 1 211 2-C-methyl-D-erythritol 4-phosphate
cytidylyltransferase. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 212 372 2-C-methyl-D-erythritol 2,4-
cyclodiphosphate synthase.
{ECO:0000256|HAMAP-Rule:MF_01520}.
REGION 218 220 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 244 245 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 248 256 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 266 268 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 271 275 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
REGION 341 345 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01520}.
METAL 218 218 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01520}.
METAL 220 220 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01520}.
METAL 252 252 Divalent metal cation.
{ECO:0000256|HAMAP-Rule:MF_01520}.
BINDING 275 275 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01520}.
BINDING 349 349 Substrate; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01520}.
BINDING 352 352 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01520}.
SITE 16 16 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SITE 23 23 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SITE 139 139 Positions MEP for the nucleophilic
attack. {ECO:0000256|HAMAP-
Rule:MF_01520}.
SITE 191 191 Positions MEP for the nucleophilic
attack. {ECO:0000256|HAMAP-
Rule:MF_01520}.
SITE 244 244 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SITE 343 343 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_01520}.
SEQUENCE 372 AA; 41579 MW; BA396402E6756A87 CRC64;
MNDTTLVLLG AGNSTRFGLK TKKQWLYIGE EPLWYFVTKQ FKKYGFKETI VVSSIQEIPY
MKKFDTFAFV EGGETRQESL KNALQNVLTK YVLVSDIARC CIDHDMIQRI LDNKEKANCI
VPALSISDTL YMDDSPANRE GAKLIQTPQL SETKLLVKAI QTDELFTDDS SAMHKSGYKI
LFVEGSQNAH KLTFASDLEK LTCLKAPSLK TFTGFGIDTH PFEQNKPMYL CGEKIEENFG
FKAHSDGDVA IHAIIDALLG AAGLGDIGEF FPDSDDKYKD IDSKELLKLC VEKVNSYGFA
INNIDITILA EIPKISPYKE KMRQTLSGIL DINQRSVNIK ATTSESLGFI GRNEGISVHA
VATLSYFNWA EI


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