(data stored in ACNUC7421 zone)

SWISSPROT: D6XV79_BACIE

ID   D6XV79_BACIE            Unreviewed;       165 AA.
AC   D6XV79;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
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   OrderedLocusNames=Bsel_0088 {ECO:0000313|EMBL:ADH97637.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97637.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97637.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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:
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}.
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DR   EMBL; CP001791; ADH97637.1; -; Genomic_DNA.
DR   RefSeq; WP_013171067.1; NC_014219.1.
DR   STRING; 439292.Bsel_0088; -.
DR   EnsemblBacteria; ADH97637; ADH97637; Bsel_0088.
DR   KEGG; bse:Bsel_0088; -.
DR   eggNOG; ENOG4108UH8; Bacteria.
DR   eggNOG; COG0245; LUCA.
DR   HOGENOM; HOG000239175; -.
DR   KO; K01770; -.
DR   OMA; DIGHYFP; -.
DR   OrthoDB; 1716560at2; -.
DR   BioCyc; BSEL439292:G1GLR-112-MONOMER; -.
DR   UniPathway; UPA00056; UER00095.
DR   Proteomes; UP000000271; 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; 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;
DR   PRODOM; D6XV79.
DR   SWISS-2DPAGE; D6XV79.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
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, ECO:0000313|EMBL:ADH97637.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00107,
KW   ECO:0000256|SAAS:SAAS01078178};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN        1    154       YgbB. {ECO:0000259|Pfam:PF02542}.
FT   REGION        8     10       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       34     35       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       38     46       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       56     58       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION       61     65       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION      100    106       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   REGION      131    135       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00107}.
FT   METAL         8      8       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        10     10       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   METAL        42     42       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING      65     65       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING     139    139       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   BINDING     142    142       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00107}.
FT   SITE         34     34       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
FT   SITE        133    133       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00107}.
SQ   SEQUENCE   165 AA;  17759 MW;  08837F1F585A2DBD CRC64;
     MRIGQGFDVH QLKEGRPLIL GGIEIPHEQG LDGHSDADVL LHTIADACLG AVAEGDIGKH
     FPDTDPAFKD ADSAKLLEHV WQIVKEKGYT LGNLDCTIMA QRPKMAPHID AMRTRIAGLL
     EADVSQINVK ATTTEKLGFT GREEGIASQA VVLLVEQPTA FTSVP
//

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