ID   CLDB_STRCP              Reviewed;         532 AA.
AC   A0A0H5BB10;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Copalyl diphosphate synthase {ECO:0000303|PubMed:26814669};
DE            EC=5.5.1.12 {ECO:0000305|PubMed:26814669};
DE   AltName: Full=Type-B diterpene synthase {ECO:0000303|PubMed:26814669};
GN   Name=cldB {ECO:0000303|PubMed:26814669};
OS   Streptomyces cyslabdanicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1470456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DOMAIN.
RC   STRAIN=DSM 42135 / NBRC 110081 / K04-0144;
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND DOMAIN.
RC   STRAIN=DSM 42135 / NBRC 110081 / K04-0144;
RX   PubMed=26814669; DOI=10.1038/ja.2015.147;
RA   Yamada Y., Komatsu M., Ikeda H.;
RT   "Chemical diversity of labdane-type bicyclic diterpene biosynthesis in
RT   Actinomycetales microorganisms.";
RL   J. Antibiot. 69:515-523(2016).
CC   -!- FUNCTION: Involved in the biosynthesis of the mercapturic acid
CC       derivative diterpene cyslabdan A, a potentiator of the beta-lactam
CC       antibiotic imipenem (PubMed:26507838). Catalyzes the conversion of
CC       geranylgeranyl diphosphate (GGDP) into (+)-copalyl diphosphate
CC       (PubMed:26507838, PubMed:26814669). {ECO:0000269|PubMed:26507838,
CC       ECO:0000269|PubMed:26814669}.
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:0000305|PubMed:26814669};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:26814669};
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, ECO:0000305|PubMed:26814669}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; LC064028; BAR97451.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5BB10; -.
DR   SMR; A0A0H5BB10; -.
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   1: Evidence at protein level;
KW   Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..532
FT                   /note="Copalyl diphosphate synthase"
FT                   /id="PRO_0000444810"
FT   MOTIF           313..318
FT                   /note="DXDDTA motif"
FT                   /evidence="ECO:0000305|PubMed:26507838,
FT                   ECO:0000305|PubMed:26814669"
FT   MOTIF           443..449
FT                   /note="QXXDGSW motif"
FT                   /evidence="ECO:0000305|PubMed:26507838,
FT                   ECO:0000305|PubMed:26814669"
SQ   SEQUENCE   532 AA;  56819 MW;  BF281A4E9B8CF2DF CRC64;
     MSSISHQAAP TRAQHTNSYV QLARQLVTSV DNDPWGDVPP SVYETARVTS WAPWLEGHER
     RLAWLLERQS AAGSWGEGPT PYRLLPTLSV TEALLSTLRQ NTAAGVSRER LAAAVDNGLA
     ALRDLSGTGG WPDTAAIEIL APDLVVLIND HLDQPEVAAL PRLGPWARGQ RLAQPHGFQA
     ALPDRVAERC QVAGGVPLKL HHTFEGVARR LPRMVPGVPG GLLGSSPAAT AAWLATGPDE
     GRDQAVTALT AVAERYDGLF PEATPISVFE RLWISVALAR PGLPAACVPT IRAWAAEIYD
     ATGVRGAPGL LPDTDDTAMA VLASALAGSP RDPSPLSAFE AGDHYDCYVG EDTGSSTANA
     HALQALTAWL SHRPATGDAL QARRDLTRDW LLAQQESDGA WRDKWHASPY YATERCVTAL
     SGHTGPTTRD AIRSAADWVL DAQSDDGSWG VWGGTAEETA YAVNILLNSP DHTGTPEATQ
     ALKLAENVLR EAVHSSGHHH PALWHDKTLY APQAMAQAEV IAALELLQAR RP