ID   RMNB_STRAQ              Reviewed;         549 AA.
AC   A0A0H5BB17;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Copalyl diphosphate synthase {ECO:0000303|PubMed:26507838};
DE            EC=5.5.1.12 {ECO:0000269|PubMed:26507838};
DE   AltName: Full=Type-B diterpene synthase {ECO:0000303|PubMed:26507838};
GN   Name=rmnB {ECO:0000303|PubMed:26507838};
OS   Streptomyces anulatus (Streptomyces chrysomallus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1892 {ECO:0000303|PubMed:26507838};
RN   [1] {ECO:0000303|PubMed:26507838}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DOMAIN.
RC   STRAIN=GM95 {ECO:0000312|EMBL:BAR97461.1};
RX   PubMed=26507838; DOI=10.1007/s10295-015-1694-6;
RA   Ikeda H., Shin-ya K., Nagamitsu T., Tomoda H.;
RT   "Biosynthesis of mercapturic acid derivative of the labdane-type diterpene,
RT   cyslabdan that potentiates imipenem activity against methicillin-resistant
RT   Staphylococcus aureus: cyslabdan is generated by mycothiol-mediated
RT   xenobiotic detoxification.";
RL   J. Ind. Microbiol. Biotechnol. 43:325-342(2016).
CC   -!- FUNCTION: Involved in the biosynthesis of the labdane-type bicyclic
CC       diterpene labda-8(17),12(E),14-triene. Catalyzes the conversion of
CC       geranylgeranyl diphosphate (GGDP) into (+)-copalyl diphosphate.
CC       {ECO:0000269|PubMed:26507838}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC         diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC         ChEBI:CHEBI:58756; EC=5.5.1.12;
CC         Evidence={ECO:0000250|UniProtKB:A0A0H5BB10};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A0A0H5BB10};
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp-Thr-Ala (DXDDTA) and Gln-Xaa-Xaa-Asp-Gly-
CC       Ser-Trp (QXXDGSW) motifs are expected to bind to Mg(2+).
CC       {ECO:0000305|PubMed:26507838}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC   -!- CAUTION: Not expressed under laboratory conditions.
CC       {ECO:0000269|PubMed:26507838}.
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DR   EMBL; LC064029; BAR97461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5BB17; -.
DR   SMR; A0A0H5BB17; -.
DR   GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; 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   3: Inferred from homology;
KW   Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..549
FT                   /note="Copalyl diphosphate synthase"
FT                   /id="PRO_0000444811"
FT   MOTIF           321..326
FT                   /note="DXDDTA motif"
FT                   /evidence="ECO:0000250|UniProtKB:D5SJ87"
FT   MOTIF           451..457
FT                   /note="QXXDGSW motif"
FT                   /evidence="ECO:0000250|UniProtKB:D5SJ87"
SQ   SEQUENCE   549 AA;  58828 MW;  A14779EEA6D072C4 CRC64;
     MTARPNPVTA TVRSDIPMSD TVVSTTYSEQ AAHLVARIDQ DGLGSVRPSL YETARVISAA
     PWLPGEPRRL AYLLDEQAPD GSWGEGPERY RLLPTLSGVE AALAVLRRGA TPTETARRLA
     GAVDRGLAAL RALPRSGPWP DTAAAEILVP GLVAKIHEQI ARIAEDGTPA LDGWRPGPGP
     ALPGGYDEAL PAYVAKRYAS VGSLPVKFHH TFEGIAGYLP PALIPDVPDL LGSSPAATAA
     RAATASSAPS AGTVAALESV AERYAGSFPE AAPILVFERL WVAAALAHTH LPAAALPTVR
     RWAADIYDPR GVRGAPGLMK DADDTAMAVL VSSLVGLEHT LEPLDQFHNG SHYDCYIGED
     TGSITANAHA LQALGGYQRR NPETQHIYGP RTDKLRDWLI DQQRPEGPWP DKWHASPYYA
     TARSVAALTR FGGGHAVTAV ETAVTWALDT QRDDGSWGVW GGTAEETAYA VQILLSTSTH
     RPQHTRALHR AETYLGDSAG SGRHPALWHD KTLYAPDAMI EAEILAARQT LRTRHDLNRR
     VTTPIHAEK