ID   A0A2S3ZQW8_9MICC        Unreviewed;       168 AA.
AC   A0A2S3ZQW8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   07-NOV-2018, entry version 4.
DE   RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS01078175};
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|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS01078202};
GN   Name=ispF {ECO:0000256|HAMAP-Rule:MF_00107};
GN   ORFNames=CVS27_20005 {ECO:0000313|EMBL:POH71625.1};
OS   Arthrobacter sp. HLT2-12-2.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1258858 {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
CC       (IPP) and dimethylallyl diphosphate (DMAPP), two major building
CC       blocks of isoprenoid compounds. Catalyzes the conversion of 4-
CC       diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to
CC       2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a
CC       corresponding release of cytidine 5-monophosphate (CMP).
CC       {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|SAAS:SAAS01078181}.
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_00107,
CC       ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS01078182}.
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.
CC       {ECO:0000256|HAMAP-Rule:MF_00107};
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_00107, ECO:0000256|SAAS:SAAS01078193}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00107,
CC       ECO:0000256|SAAS:SAAS01078180}.
CC   -!- SIMILARITY: Belongs to the IspF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00107, ECO:0000256|RuleBase:RU004395,
CC       ECO:0000256|SAAS:SAAS01078179}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00107}.
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:POH71625.1}.
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DR   EMBL; PPXC01000027; POH71625.1; -; Genomic_DNA.
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   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   Complete proteome {ECO:0000313|Proteomes:UP000237061};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00107,
KW   ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS01078191};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00107, ECO:0000256|RuleBase:RU004395,
KW   ECO:0000256|SAAS:SAAS01078177};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00107,
KW   ECO:0000256|SAAS:SAAS01078178};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237061}.
FT   DOMAIN        5    157       YgbB. {ECO:0000259|Pfam:PF02542}.
FT   REGION       11     13       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       40     41       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       44     52       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       62     64       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION      134    138       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   METAL        11     11       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        13     13       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        48     48       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING     142    142       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING     145    145       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00107}.
FT   SITE         40     40       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   SITE        136    136       Transition state stabilizer.
FT                                {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
//