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}.
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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
//