ID ISPF_CHLTB Reviewed; 178 AA.
AC B0BC71;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 46.
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=CTLon_0689;
OS Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCH-1/proctitis;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J.,
RA Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H.,
RA Harris B., Ormond D., Rance R., Quail M.A., Parkhill J.,
RA Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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.
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DR EMBL; AM884177; CAP07086.1; -; Genomic_DNA.
DR RefSeq; YP_001653777.1; NC_010280.2.
DR ProteinModelPortal; B0BC71; -.
DR STRING; 471473.CTLon_0689; -.
DR EnsemblBacteria; CAP07086; CAP07086; CTLon_0689.
DR GeneID; 5858993; -.
DR KEGG; ctl:CTLon_0689; -.
DR PATRIC; 20383043; VBIChlTra68089_0747.
DR eggNOG; COG0245; -.
DR HOGENOM; HOG000239175; -.
DR KO; K01770; -.
DR OMA; GYGEDSH; -.
DR ProtClustDB; PRK00084; -.
DR BioCyc; CTRA471473:GHJK-689-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 1 178 2-C-methyl-D-erythritol 2,4-
FT cyclodiphosphate synthase.
FT /FTId=PRO_1000094251.
FT REGION 24 26 Substrate binding (By similarity).
FT REGION 57 65 Substrate binding (By similarity).
FT REGION 149 153 Substrate binding (By similarity).
FT METAL 24 24 Divalent metal cation (By similarity).
FT METAL 26 26 Divalent metal cation (By similarity).
FT METAL 61 61 Divalent metal cation (By similarity).
FT SITE 53 53 Transition state stabilizer (By
FT similarity).
FT SITE 151 151 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 178 AA; 19460 MW; 373EAA5E2AF54476 CRC64;
MTEIPSSFVL PDPEWIYRVG IGQDSHRFLP DEDPKPCILG GIIFENTPGF EANSDGDVVF
HAICNAFSSV THKGILGGLA DELLKTKGIT DSVVYLQEAI ASLKPTQRVS HLAITIEGKR
PKLLPQLPSM RKRIAEVLHI PLDSINITAT SGEGLTAMGQ GYGVQCFCVL TIMEYCRY
//
