ID   ECDPS_STREO             Reviewed;         511 AA.
AC   Q5KSN5;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Ent-copalyl diphosphate synthase {ECO:0000303|PubMed:17148547};
DE            Short=Ent-CDP synthase {ECO:0000303|PubMed:17148547};
DE            EC=5.5.1.13 {ECO:0000269|PubMed:17148547};
GN   Name=ent-cdps {ECO:0000312|EMBL:BAD86797.1};
OS   Streptomyces sp. (strain KO-3988).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=285219;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=KO-3988;
RX   PubMed=15712669; DOI=10.7164/antibiotics.57.739;
RA   Kawasaki T., Kuzuyama T., Kuwamori Y., Matsuura N., Itoh N., Furihata K.,
RA   Seto H., Dairi T.;
RT   "Presence of copalyl diphosphate synthase gene in an actinomycete
RT   possessing the mevalonate pathway.";
RL   J. Antibiot. 57:739-747(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=KO-3988;
RX   PubMed=17148547; DOI=10.1093/jb/mvm004;
RA   Ikeda C., Hayashi Y., Itoh N., Seto H., Dairi T.;
RT   "Functional analysis of eubacterial ent-copalyl diphosphate synthase and
RT   pimara-9(11),15-diene synthase with unique primary sequences.";
RL   J. Biochem. 141:37-45(2007).
CC   -!- FUNCTION: Involved in viguiepinol biosynthesis. Catalyzes the
CC       conversion of geranylgeranyl diphosphate (GGDP) into copalyl
CC       diphosphate (ent-CDP). {ECO:0000269|PubMed:15712669,
CC       ECO:0000269|PubMed:17148547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl
CC         diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553,
CC         ChEBI:CHEBI:58756; EC=5.5.1.13;
CC         Evidence={ECO:0000269|PubMed:17148547};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|PubMed:17148547};
CC       Note=Activity is highest with Mg(2+). Can also use Zn(2+), Co(2+),
CC       Mn(2+) and Ni(2+). {ECO:0000269|PubMed:17148547};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.7 uM for GGDP {ECO:0000269|PubMed:17148547};
CC         Note=kcat is 0.033 sec(-1). {ECO:0000269|PubMed:17148547};
CC       pH dependence:
CC         Optimum pH is 5.5. {ECO:0000269|PubMed:17148547};
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.
CC         {ECO:0000269|PubMed:17148547};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17148547}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AB183750; BAD86797.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KSN5; -.
DR   SMR; Q5KSN5; -.
DR   GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR032696; SQ_cyclase_C.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF00432; Prenyltrans; 1.
DR   Pfam; PF13243; SQHop_cyclase_C; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Isomerase; Metal-binding.
FT   CHAIN           1..511
FT                   /note="Ent-copalyl diphosphate synthase"
FT                   /id="PRO_0000431697"
FT   MOTIF           291..294
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         291
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         293
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
SQ   SEQUENCE   511 AA;  54768 MW;  7575266A78333C6D CRC64;
     MNVTSFAALR AAAQDIVDEM IADPYGLTSP SVYETARMVV SAPWLEGHRQ RVEFLLAQQH
     EDGTWGGPAA YGLLPTLSAV DALLSVAGTQ DARRVAGAVE SGLAALAGRF PRNVELPDTI
     AVELLVPWLI EQVDQRLSRM DDRGDLPGRL DLQADTGTLS GIRELLRQNT GIPEKTWHSL
     EALGAPAVRS GTVTPMGGAV GASPAATSAW LGDPPHTDAA KACLAYLHQT QARHGGPVSG
     ITSISYFELA WVVTALSGSG LDVDIPAQVP DILRTALGAN GLSAGPGLPA DSDDTSAALH
     ALDLLGKPES VDCLWEYDTG LYFTCFPKER TPSTSTNAHI LVALADRRGQ GDTRYDHAAE
     RVGGWLVEQQ QPDGRWMDKW HASPYYATAC GAAAMARLDG PRTSAALDDA IRWVLDTQHA
     DGSWGRWEGT GEETAYALQV LNHRAAPDRP ALEAIRAGRA FLSGHVEDDR RNPPLWHDKD
     LYTPVRVIRA EILGTLAATQ RLAEAEKEAR A