ID A0A2S3ZQW8_ARTGL Unreviewed; 168 AA. AC A0A2S3ZQW8; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 29-SEP-2021, entry version 14. DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|ARBA:ARBA00014197, 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 ORFNames=CVS27_20005 {ECO:0000313|EMBL:POH71625.1}; OS Arthrobacter glacialis. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter. OX NCBI_TaxID=1664 {ECO:0000313|EMBL:POH71625.1, ECO:0000313|Proteomes:UP000237061}; RN [1] {ECO:0000313|EMBL:POH71625.1, ECO:0000313|Proteomes:UP000237061} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HLT2-12-2 {ECO:0000313|EMBL:POH71625.1, RC ECO:0000313|Proteomes:UP000237061}; RA Liu Q., Xin Y.-H.; RT "Arthrobacter sp. nov., from glaciers in China."; RL Submitted (JAN-2018) 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|HAMAP-Rule:MF_00107}. CC -!- SIMILARITY: Belongs to the IspF family. {ECO:0000256|HAMAP- CC Rule:MF_00107, ECO:0000256|RuleBase:RU004395}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00107}. 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:POH71625.1}. 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; PPXC01000027; POH71625.1; -; Genomic_DNA. DR EnsemblBacteria; POH71625; POH71625; CVS27_20005. DR UniPathway; UPA00056; UER00095. DR Proteomes; UP000237061; Unassembled WGS sequence. 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-UniPathway. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00554; MECDP_synthase; 1. DR Gene3D; 3.30.1330.50; -; 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 PANTHER; PTHR43181; PTHR43181; 1. DR Pfam; PF02542; YgbB; 1. DR SUPFAM; SSF69765; SSF69765; 1. DR TIGRFAMs; TIGR00151; ispF; 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}; Reference proteome {ECO:0000313|Proteomes:UP000237061}. FT DOMAIN 5..157 FT /note="YgbB" FT /evidence="ECO:0000259|Pfam:PF02542" FT REGION 11..13 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT REGION 40..41 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT REGION 44..52 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT REGION 62..64 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT REGION 134..138 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT METAL 11 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT METAL 13 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT METAL 48 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 142 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT BINDING 145 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT SITE 40 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" FT SITE 136 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00107" SQ SEQUENCE 168 AA; 17041 MW; 39E4F435EC610241 CRC64; MILPRTGIGV DIHAFAPEDS PAPLWLAGLF WEGERGLSGH SDGDAVAHAA ADALFSAAGV GDLGTHFGTD RPEYKGASGV TLLAEAARIV RAAGFEIGNV AVQFVGNRPI FSPRRQEAEA VLSAAAGAPV SVSATTSDKL GFPGRGEGIT AIATALVIQN APASAPER //