ID A0A0A0HRL0_9RHOB Unreviewed; 380 AA. AC A0A0A0HRL0; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 12-AUG-2020, entry version 46. DE RecName: Full=Bifunctional enzyme IspD/IspF {ECO:0000256|HAMAP-Rule:MF_01520}; DE Includes: DE RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520}; DE EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_01520}; DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_01520}; DE AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520}; DE Short=MCT {ECO:0000256|HAMAP-Rule:MF_01520}; DE Includes: DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01520}; DE Short=MECDP-synthase {ECO:0000256|HAMAP-Rule:MF_01520}; DE Short=MECPP-synthase {ECO:0000256|HAMAP-Rule:MF_01520}; DE Short=MECPS {ECO:0000256|HAMAP-Rule:MF_01520}; DE EC=4.6.1.12 {ECO:0000256|HAMAP-Rule:MF_01520}; GN Name=ispDF {ECO:0000256|HAMAP-Rule:MF_01520}; GN ORFNames=rosmuc_01566 {ECO:0000313|EMBL:KGM88728.1}; OS Roseovarius mucosus DSM 17069. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Roseovarius. OX NCBI_TaxID=1288298 {ECO:0000313|EMBL:KGM88728.1, ECO:0000313|Proteomes:UP000030021}; RN [1] {ECO:0000313|EMBL:KGM88728.1, ECO:0000313|Proteomes:UP000030021} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17069 {ECO:0000313|EMBL:KGM88728.1, RC ECO:0000313|Proteomes:UP000030021}; RA Fiebig A., Goeker M., Klenk H.-P.P.; RL Submitted (JAN-2013) 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-D- CC erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- CC diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- CC methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding CC release of cytidine 5-monophosphate (CMP) (IspF). {ECO:0000256|HAMAP- CC Rule:MF_01520}. CC -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- CC erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). CC {ECO:0000256|ARBA:ARBA00002459}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C- CC methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, CC ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60; CC Evidence={ECO:0000256|ARBA:ARBA00001282, ECO:0000256|HAMAP- CC Rule:MF_01520}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D- CC erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864, CC ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377; EC=4.6.1.12; CC Evidence={ECO:0000256|ARBA:ARBA00000200, ECO:0000256|HAMAP- CC Rule:MF_01520}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|ARBA:ARBA00001968, CC ECO:0000256|HAMAP-Rule:MF_01520}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5- CC phosphate: step 4/6. {ECO:0000256|ARBA:ARBA00004709, ECO:0000256|HAMAP- CC Rule:MF_01520}. CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD CC subfamily. {ECO:0000256|ARBA:ARBA00009789}. CC -!- SIMILARITY: Belongs to the IspF family. CC {ECO:0000256|ARBA:ARBA00008480}. CC -!- SIMILARITY: In the C-terminal section; belongs to the IspF family. CC {ECO:0000256|HAMAP-Rule:MF_01520}. CC -!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI CC cytidylyltransferase family. IspD subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01520}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01520}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KGM88728.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AONH01000007; KGM88728.1; -; Genomic_DNA. DR STRING; 1288298.rosmuc_01566; -. DR EnsemblBacteria; KGM88728; KGM88728; rosmuc_01566. DR PATRIC; fig|1288298.3.peg.1577; -. DR eggNOG; COG0245; Bacteria. DR eggNOG; COG1211; Bacteria. DR HOGENOM; CLU_042800_2_3_5; -. DR UniPathway; UPA00056; UER00095. DR Proteomes; UP000030021; Unassembled WGS sequence. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd02516; CDP-ME_synthetase; 1. DR CDD; cd00554; MECDP_synthase; 1. DR Gene3D; 3.30.1330.50; -; 1. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00108; IspD; 1. DR HAMAP; MF_01520; IspDF; 1. DR HAMAP; MF_00107; IspF; 1. DR InterPro; IPR001228; IspD. DR InterPro; IPR026596; IspD/F. DR InterPro; IPR034683; IspD/TarI. DR InterPro; IPR018294; ISPD_synthase_CS. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. DR InterPro; IPR036571; MECDP_synthase_sf. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01128; IspD; 1. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR SUPFAM; SSF69765; SSF69765; 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 Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP- KW Rule:MF_01520}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000313|EMBL:KGM88728.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01520}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01520}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000313|EMBL:KGM88728.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000030021}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000313|EMBL:KGM88728.1}. FT DOMAIN 222..375 FT /note="YgbB" FT /evidence="ECO:0000259|Pfam:PF02542" FT REGION 1..222 FT /note="2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT REGION 223..380 FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate FT synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT REGION 229..231 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT REGION 255..256 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT REGION 259..267 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT REGION 277..279 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT REGION 352..356 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT METAL 229 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT METAL 231 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT METAL 263 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT BINDING 286 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT BINDING 360 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT BINDING 363 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT SITE 15 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT SITE 22 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT SITE 149 FT /note="Positions MEP for the nucleophilic attack" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT SITE 202 FT /note="Positions MEP for the nucleophilic attack" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT SITE 255 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" FT SITE 354 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01520" SQ SEQUENCE 380 AA; 40516 MW; B76D532CA7D82AB6 CRC64; MTTAALIVAA GRGTRAGGDC PKQWQPLLGR RVIDWTLDAF LGAEGIDRIL VVLHPDDLDR LAPDPRILVT TGGATRAESV RNGLEVLASD PPDHVLIHDV ARCCTKSPYI AYITYKIRST GLPALAPALP VTDALWTGVD GRVTGTRDRT GLYRAQTPQA FDFTSIIAAH RAHEGDAADD VAVARAAGID VTILDGDEDN LKITHPHDFK RAEKILGNQM DIRVGSGFDV HRFGPGDHCM LCGVAVPHDR GLQGHSDADV GLHALADAIY GGLAQGDIGR HFPPSDPQWK GAKSHIFLRH AVGLADELGF KINNIDVTLV CERPKITPHA PAMQAALSEI TGIAPDRISV KATTSERLGF TGREEGIAAQ AVVTLVKPCA //