ID A0A381CRW9_CAMJU Unreviewed; 371 AA. AC A0A381CRW9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, entry version 2. 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=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}; GN Name=ispDF {ECO:0000256|HAMAP-Rule:MF_01520, GN ECO:0000313|EMBL:SUW91978.1}; GN ORFNames=NCTC13105_00601 {ECO:0000313|EMBL:SUW91978.1}; OS Campylobacter jejuni. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=197 {ECO:0000313|EMBL:SUW91978.1, ECO:0000313|Proteomes:UP000254131}; RN [1] {ECO:0000313|EMBL:SUW91978.1, ECO:0000313|Proteomes:UP000254131} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC13105 {ECO:0000313|EMBL:SUW91978.1, RC ECO:0000313|Proteomes:UP000254131}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) 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: CC Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP- CC 2-C-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|HAMAP-Rule:MF_01520, CC ECO:0000256|SAAS:SAAS00709147}; 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; CC EC=4.6.1.12; Evidence={ECO:0000256|HAMAP-Rule:MF_01520, CC ECO:0000256|SAAS:SAAS01078182}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01520, CC ECO:0000256|SAAS:SAAS01078176}; 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:SAAS01078193}. 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 --------------------------------------------------------------------------- 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; UFVB01000001; SUW91978.1; -; Genomic_DNA. DR UniPathway; UPA00056; UER00093. DR Proteomes; UP000254131; Unassembled WGS sequence. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. 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_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:UP000254131}; KW Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS01078191}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS01078177}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS01078178}; 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:SUW91978.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01520, KW ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:SUW91978.1}. FT DOMAIN 211 363 YgbB. {ECO:0000259|Pfam:PF02542}. FT REGION 1 210 2-C-methyl-D-erythritol 4-phosphate FT cytidylyltransferase. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 211 371 2-C-methyl-D-erythritol 2,4- FT cyclodiphosphate synthase. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT REGION 217 219 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 243 244 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 247 255 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 265 267 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 270 274 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT REGION 340 344 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01520}. FT METAL 217 217 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT METAL 219 219 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT METAL 251 251 Divalent metal cation. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 274 274 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 348 348 Substrate; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT BINDING 351 351 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 16 16 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 23 23 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 139 139 Positions MEP for the nucleophilic FT attack. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 191 191 Positions MEP for the nucleophilic FT attack. {ECO:0000256|HAMAP-Rule: FT MF_01520}. FT SITE 243 243 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. FT SITE 342 342 Transition state stabilizer. FT {ECO:0000256|HAMAP-Rule:MF_01520}. SQ SEQUENCE 371 AA; 41671 MW; 9FC2DE7A13355505 CRC64; MSEISLIMLA AGNSTRFNTK VKKQFLRLGN DPLWLYATKN LSSFYPFKKI VVTSSNITYM KKFTKNYEFI EGGDTRAESL KKALELIDSE FVMVSDVARV LVSKNLFDRL IENLDKADCI TPALKVADTT LFDNEALQRE KIKLIQTPQI SKTKLLKKAL DQNLEFTDDS TAIAAMGGKI WFVEGEENAR KLTFKEDLKK LDLPTPSFEI FTGNGFDVHE FGENRPLLLA GVQIHPTMGL KAHSDGDVLA HSLTDAILGA AGLGDIGELY PDTDMKFKNA NSMELLKQAY NKVREIGFEL INIDICVMAQ SPKLKDFKQA MQSNIAHTLD LDEFRINVKA TTTEKLGFIG RKEGMAVLSS VNLKYFDWTR L //