ID   PMDS_STREO              Reviewed;         295 AA.
AC   Q5KSN4;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Ent-pimara-9(11),15-diene synthase {ECO:0000303|PubMed:17148547};
DE            Short=PMD synthase {ECO:0000303|PubMed:17148547};
DE            EC=4.2.3.31 {ECO:0000269|PubMed:17148547};
OS   Streptomyces sp. (strain KO-3988).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=285219;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   PROBABLE FUNCTION.
RC   STRAIN=KO-3988;
RX   PubMed=16452404; DOI=10.1128/jb.188.4.1236-1244.2006;
RA   Kawasaki T., Hayashi Y., Kuzuyama T., Furihata K., Itoh N., Seto H.,
RA   Dairi T.;
RT   "Biosynthesis of a natural polyketide-isoprenoid hybrid compound,
RT   furaquinocin A: identification and heterologous expression of the gene
RT   cluster.";
RL   J. Bacteriol. 188:1236-1244(2006).
RN   [3]
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 copalyl diphosphate (ent-CDP) into pimara-9(11),15-diene
CC       (PMD). {ECO:0000269|PubMed:16452404, ECO:0000269|PubMed:17148547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ent-copalyl diphosphate = diphosphate + ent-pimara-9(11),15-
CC         diene; Xref=Rhea:RHEA:25544, ChEBI:CHEBI:33019, ChEBI:CHEBI:50064,
CC         ChEBI:CHEBI:58553; EC=4.2.3.31;
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 Co(2+), Zn(2+) and
CC       Ni(2+). {ECO:0000269|PubMed:17148547};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.6 uM for ent-CDP {ECO:0000269|PubMed:17148547};
CC         Note=kcat is 0.0014 sec(-1). {ECO:0000269|PubMed:17148547};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:17148547};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:17148547};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17148547}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; AB183750; BAD86798.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KSN4; -.
DR   SMR; Q5KSN4; -.
DR   KEGG; ag:BAD86798; -.
DR   BioCyc; MetaCyc:MON-13867; -.
DR   GO; GO:0052674; F:ent-pimara-9(11),15-diene synthase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Lyase.
FT   CHAIN           1..295
FT                   /note="Ent-pimara-9(11),15-diene synthase"
FT                   /id="PRO_0000431698"
SQ   SEQUENCE   295 AA;  32795 MW;  F40BF1D7D3F19107 CRC64;
     MRARHRVALK VLADLRSWAA EYPQVLEATP IEALAISTAA ISPWRGANEL RLSAPDVRCG
     PTPLDDHVEQ NVRSLDELDD LFGRCEAIVR GGDRDDGHPL LASLSGWQSA LERAPHYPKL
     AGLWGDRFAE ALRGERYDWT AGLARDRGEG PSDPQEYLTY AASSNAWITH FPRWATSDRD
     DLLDGLPVLD NALEAIEVAV RLSNDLATFE RERAEPGQNN ILMYDTSPDW VHDELDRHSR
     KAQEQLDPLA TAGFPPAVEL LRLLDWSVTF YSGADFRGWG SDRDLTGPSG LPSDM