ID A0A0D6Q9J5_KOMXY Unreviewed; 396 AA. AC A0A0D6Q9J5; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 28-FEB-2018, entry version 28. DE RecName: Full=Bifunctional enzyme IspD/IspF {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}; 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}; GN Name=ispDF {ECO:0000256|HAMAP-Rule:MF_01520}; GN ORFNames=Gxy13693_024_061 {ECO:0000313|EMBL:GAN99645.1}; OS Komagataeibacter xylinus NBRC 13693. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Acetobacteraceae; Komagataeibacter. OX NCBI_TaxID=1234668 {ECO:0000313|EMBL:GAN99645.1, ECO:0000313|Proteomes:UP000032683}; RN [1] {ECO:0000313|EMBL:GAN99645.1, ECO:0000313|Proteomes:UP000032683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 13693 {ECO:0000313|EMBL:GAN99645.1, RC ECO:0000313|Proteomes:UP000032683}; RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.; RT "Whole genome sequence of Gluconacetobacter xylinus NBRC 13693."; RL Submitted (NOV-2012) 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:SAAS00771987}. 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:SAAS00771955}. 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:SAAS00709147}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01520, CC ECO:0000256|SAAS:SAAS00771949}; 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:SAAS00709253}. 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:SAAS00771963}. CC -!- SIMILARITY: In the C-terminal section; belongs to the IspF family. CC {ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|SAAS:SAAS00771954}. 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:SAAS00771938}. 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:GAN99645.1}. 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; BANJ01000024; GAN99645.1; -; Genomic_DNA. DR EnsemblBacteria; GAN99645; GAN99645; Gxy13693_024_061. DR UniPathway; UPA00056; UER00093. DR Proteomes; UP000032683; 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 Complete proteome {ECO:0000313|Proteomes:UP000032683}; KW Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00771928}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00771989}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00771962}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00771957}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00981526, ECO:0000313|EMBL:GAN99645.1}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:GAN99645.1}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 396 Bifunctional enzyme IspD/IspF. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002310832. FT DOMAIN 241 393 YgbB. {ECO:0000259|Pfam:PF02542}. FT REGION 1 240 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 241 396 2-C-methyl-D-erythritol 2,4- FT cyclodiphosphate synthase. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT REGION 247 249 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 273 274 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 277 285 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 295 297 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 370 374 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT METAL 247 247 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT METAL 249 249 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT METAL 281 281 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 378 378 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 381 381 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 22 22 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 33 33 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 166 166 Positions MEP for the nucleophilic FT attack. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 220 220 Positions MEP for the nucleophilic FT attack. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 273 273 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 372 372 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. SQ SEQUENCE 396 AA; 41962 MW; 32DA45C49511BAA2 CRC64; MAALLRIMRV AAILLAAGQG SRYSAQTATP LAKQYVTLGG RPVIRHAADA LAPHVGMIQP VGDPALLTGA LEGFAPAGCT VLPVVPGGAT RQASVSAGLE ALDRLPEDRR PDLVLIHDGA RPYVPADVTQ GVIAALEQHA GVIPAVPVAD TIKRAKDGII TDTVPRTDLF RAQTPQGFRF ALLRDLHRAA DAADATDDAA LLEQAGHHVA IVPGSEDNIK LTYKEDLVRL ERLIGPTLLP RTGMGYDVHA FAENRPLIMC GINVPHTRGL AGHSDADVGI HALCDAIYGA LAEGDIGRHF PPSQNEWKDA DSARFLVHAG ERIRLRGGML VNADVTLICE RPKIGPHSEA MRARLADLLK VDVDRISVKA TTSERLGFTG REEGIACLAS ATVLVP //