ID A0A0A0HRL0_9RHOB Unreviewed; 380 AA. AC A0A0A0HRL0; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 15-MAR-2017, entry version 20. 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=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520}; DE Short=MCT {ECO:0000256|HAMAP-Rule:MF_01520}; DE AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {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- CC D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the CC conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2- CC phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4- CC cyclodiphosphate (ME-CPP) with a corresponding release of cytidine CC 5-monophosphate (CMP) (IspF). {ECO:0000256|HAMAP-Rule:MF_01520, CC ECO:0000256|SAAS:SAAS00096234}. CC -!- CATALYTIC ACTIVITY: 2-phospho-4-(cytidine 5'-diphospho)-2-C- CC methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate CC + CMP. {ECO:0000256|HAMAP-Rule:MF_01520, CC ECO:0000256|SAAS:SAAS00652832}. CC -!- CATALYTIC ACTIVITY: CTP + 2-C-methyl-D-erythritol 4-phosphate = CC diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. CC {ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|SAAS:SAAS00096256}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01520, CC ECO:0000256|SAAS:SAAS00652830}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000256|HAMAP- CC Rule:MF_01520, ECO:0000256|SAAS:SAAS00388668}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000256|HAMAP- CC Rule:MF_01520, ECO:0000256|SAAS:SAAS00652827}. CC -!- SIMILARITY: In the C-terminal section; belongs to the IspF family. CC {ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|SAAS:SAAS00574066}. CC -!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI CC cytidylyltransferase family. IspD subfamily. {ECO:0000256|HAMAP- CC Rule:MF_01520, ECO:0000256|SAAS:SAAS00628227}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01520}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 RefSeq; WP_037271707.1; NZ_KN293978.1. DR EnsemblBacteria; KGM88728; KGM88728; rosmuc_01566. DR UniPathway; UPA00056; UER00093. DR Proteomes; UP000030021; Unassembled WGS sequence. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-HAMAP. 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-HAMAP. 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; IPR018294; ISPD_synthase_CS. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. 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 Complete proteome {ECO:0000313|Proteomes:UP000030021}; KW Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00652821}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|SAAS:SAAS00652819, KW ECO:0000313|EMBL:KGM88728.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00652813}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00096233}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00658167, ECO:0000313|EMBL:KGM88728.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00658169, ECO:0000313|EMBL:KGM88728.1}. FT DOMAIN 222 375 YgbB. {ECO:0000259|Pfam:PF02542}. FT REGION 1 222 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 223 380 2-C-methyl-D-erythritol 2,4- FT cyclodiphosphate synthase. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT REGION 229 231 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 255 256 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 259 267 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 277 279 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 352 356 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT METAL 229 229 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT METAL 231 231 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT METAL 263 263 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 286 286 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 360 360 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 363 363 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 15 15 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 22 22 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 149 149 Positions MEP for the nucleophilic FT attack. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 202 202 Positions MEP for the nucleophilic FT attack. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 255 255 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 354 354 Transition state stabilizer. FT {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 //