(data stored in ACNUC7421 zone)

SWISSPROT: E3J8M4_FRAIE

ID   E3J8M4_FRAIE            Unreviewed;       172 AA.
AC   E3J8M4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   16-JAN-2019, entry version 59.
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:SAAS01078202};
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   OrderedLocusNames=FraEuI1c_0381 {ECO:0000313|EMBL:ADP78467.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78467.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78467.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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}.
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_00107,
CC         ECO:0000256|RuleBase:RU004395, ECO:0000256|SAAS:SAAS01115720};
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}.
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DR   EMBL; CP002299; ADP78467.1; -; Genomic_DNA.
DR   RefSeq; WP_013421589.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0381; -.
DR   EnsemblBacteria; ADP78467; ADP78467; FraEuI1c_0381.
DR   KEGG; fri:FraEuI1c_0381; -.
DR   eggNOG; ENOG4108UH8; Bacteria.
DR   eggNOG; COG0245; LUCA.
DR   HOGENOM; HOG000239175; -.
DR   KO; K01770; -.
DR   OMA; DIGHYFP; -.
DR   OrthoDB; 1716560at2; -.
DR   BioCyc; FSP298654:G1GOT-382-MONOMER; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000002484; 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-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; IPR036571; MECDP_synthase_sf.
DR   Pfam; PF02542; YgbB; 1.
DR   SUPFAM; SSF69765; SSF69765; 1.
DR   TIGRFAMs; TIGR00151; ispF; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J8M4.
DR   SWISS-2DPAGE; E3J8M4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
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:UP000002484}.
FT   DOMAIN       17    167       YgbB. {ECO:0000259|Pfam:PF02542}.
FT   REGION       23     25       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       49     50       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       53     61       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       71     73       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION      144    148       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   METAL        23     23       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        25     25       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        57     57       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING     155    155       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00107}.
FT   SITE         49     49       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   SITE        146    146       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
SQ   SEQUENCE   172 AA;  16980 MW;  47BAF4C46F366922 CRC64;
     MAAGVTPATA AAIALPRVGV GVDVHPFEQG RPCWVACLQW DGETGLAGHS DGDVAAHAAC
     DALLIASGLG DLGKVFGTDR PEWSGASGAA LLGETARLLA EDGWTIGNVA VQVVGNRPRM
     AKRRDEAAAA MATALGGAVV SVSATTTDGL GLTGRGEGLA AIATALVARL AG
//

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