ID A0AAD1NN54_9GAMM Unreviewed; 159 AA. AC A0AAD1NN54; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 02-OCT-2024, entry version 3. DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|ARBA:ARBA00012579, ECO:0000256|HAMAP-Rule:MF_00107}; DE Short=MECDP-synthase {ECO:0000256|HAMAP-Rule:MF_00107}; DE Short=MECPP-synthase {ECO:0000256|HAMAP-Rule:MF_00107}; DE Short=MECPS {ECO:0000256|HAMAP-Rule:MF_00107}; DE EC=4.6.1.12 {ECO:0000256|ARBA:ARBA00012579, ECO:0000256|HAMAP-Rule:MF_00107}; GN Name=ispF {ECO:0000256|HAMAP-Rule:MF_00107, GN ECO:0000313|EMBL:BCV45858.1}; GN ORFNames=TUM17379_28760 {ECO:0000313|EMBL:BCV45858.1}; OS Shewanella algae. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=38313 {ECO:0000313|EMBL:BCV45858.1, ECO:0000313|Proteomes:UP000825078}; RN [1] {ECO:0000313|EMBL:BCV45858.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TUM17379 {ECO:0000313|EMBL:BCV45858.1}; RA Ohama Y., Aoki K., Harada S., Moriya K., Ishii Y., Tateda K.; RT "Molecular characterization for Shewanella algae harboring chromosomal RT blaOXA-55-like strains isolated from clinical and environment sample."; RL Submitted (MAY-2021) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) CC and dimethylallyl diphosphate (DMAPP), two major building blocks of CC isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- CC C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol CC 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine CC 5-monophosphate (CMP). {ECO:0000256|HAMAP-Rule:MF_00107}. 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_00107, ECO:0000256|RuleBase:RU004395}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00107}; CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00107}; 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_00107}. CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233, ECO:0000256|HAMAP- CC Rule:MF_00107}. CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000256|ARBA:ARBA00008480, CC ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395}. 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; AP024613; BCV45858.1; -; Genomic_DNA. DR RefSeq; WP_071239239.1; NZ_MBFW01000064.1. DR KEGG; salg:BS332_00185; -. DR Proteomes; UP000825078; Chromosome. DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase 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-UniRule. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro. DR CDD; cd00554; MECDP_synthase; 1. DR Gene3D; 3.30.1330.50; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; 1. DR HAMAP; MF_00107; IspF; 1. DR InterPro; IPR003526; MECDP_synthase. DR InterPro; IPR020555; MECDP_synthase_CS. DR InterPro; IPR036571; MECDP_synthase_sf. DR NCBIfam; TIGR00151; ispF; 1. DR PANTHER; PTHR43181; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR43181:SF1; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; IpsF-like; 1. DR PROSITE; PS01350; ISPF; 1. PE 3: Inferred from homology; KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP- KW Rule:MF_00107}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00107}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00107}. FT DOMAIN 3..156 FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate FT synthase" FT /evidence="ECO:0000259|Pfam:PF02542" FT BINDING 10..12 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 10 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 12 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 36..37 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 44 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 58..60 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 63..67 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 102..108 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 134..137 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 141 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 144 FT /ligand="4-CDP-2-C-methyl-D-erythritol 2-phosphate" FT /ligand_id="ChEBI:CHEBI:57919" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT SITE 36 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT SITE 135 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" SQ SEQUENCE 159 AA; 17079 MW; 7F465333E909328D CRC64; MNIRIGHGFD VHKFGGEPPL VLGGVKVPYH TGLLAHSDGD VVLHAISDAI LGAMALGDIG KHFPDTDAEF KGADSRVLLR HCYRLALDKG FRLGNLDVTI IAQAPKMAPH IEAIRQMLAE DLHTDLDSIN VKATTTEKLG FTGRSEGIAV EAVVLMFGM //