ID ISPF_PSEF5 Reviewed; 157 AA.
AC Q4KHF0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 01-MAY-2013, entry version 52.
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase;
DE Short=MECDP-synthase;
DE Short=MECPP-synthase;
DE Short=MECPS;
DE EC=4.6.1.12;
GN Name=ispF; OrderedLocusNames=PFL_1202;
OS Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf-5 / ATCC BAA-477;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas
RT fluorescens Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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) (By
CC similarity).
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.
CC -!- COFACTOR: Binds 1 divalent metal cation per subunit (By
CC similarity).
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC deoxy-D-xylulose 5-phosphate: step 4/6.
CC -!- SUBUNIT: Homotrimer (By similarity).
CC -!- SIMILARITY: Belongs to the IspF family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000076; AAY90489.1; -; Genomic_DNA.
DR RefSeq; YP_258333.1; NC_004129.6.
DR ProteinModelPortal; Q4KHF0; -.
DR SMR; Q4KHF0; 1-156.
DR STRING; 220664.PFL_1202; -.
DR EnsemblBacteria; AAY90489; AAY90489; PFL_1202.
DR GeneID; 3476834; -.
DR KEGG; pfl:PFL_1202; -.
DR PATRIC; 19871611; VBIPseFlu72549_1234.
DR eggNOG; COG0245; -.
DR HOGENOM; HOG000239175; -.
DR KO; K01770; -.
DR OMA; HKFGGEG; -.
DR ProtClustDB; PRK00084; -.
DR BioCyc; PFLU220664:GIX8-1207-MONOMER; -.
DR UniPathway; UPA00056; UER00095.
DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, mevalonate-independent pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:HAMAP.
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 Pfam; PF02542; YgbB; 1.
DR SUPFAM; SSF69765; YgbB_synth; 1.
DR TIGRFAMs; TIGR00151; ispF; 1.
DR PROSITE; PS01350; ISPF; 1.
PE 3: Inferred from homology;
KW Complete proteome; Isoprene biosynthesis; Lyase; Metal-binding.
FT CHAIN 1 157 2-C-methyl-D-erythritol 2,4-
FT cyclodiphosphate synthase.
FT /FTId=PRO_0000237742.
FT REGION 8 10 Substrate binding (By similarity).
FT REGION 34 35 Substrate binding (By similarity).
FT REGION 38 46 Substrate binding (By similarity).
FT REGION 56 58 Substrate binding (By similarity).
FT REGION 61 65 Substrate binding (By similarity).
FT REGION 100 106 Substrate binding (By similarity).
FT REGION 131 135 Substrate binding (By similarity).
FT METAL 8 8 Divalent metal cation (By similarity).
FT METAL 10 10 Divalent metal cation (By similarity).
FT METAL 42 42 Divalent metal cation (By similarity).
FT BINDING 65 65 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 139 139 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 142 142 Substrate (By similarity).
FT SITE 34 34 Transition state stabilizer (By
FT similarity).
FT SITE 133 133 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 157 AA; 16928 MW; EFE8F62AECA63A32 CRC64;
MRIGHGYDVH RFAEGDFITL GGVRIAHHFG LLAHSDGDVL LHALSDALLG AAALGDIGKH
FPDTDPQFKG ADSRVLLRHV VALIHAKGWK IGNVDNTIVA QAPKMAPHIE TMRALIAEDL
QVELDQVNVK ATTTEKLGFV GREEGIAVHS VALLQRP
//
