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CLDS_TOBAC
ID   CLDS_TOBAC              Reviewed;         802 AA.
AC   G3CCC0;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Copal-8-ol diphosphate hydratase, chloroplastic {ECO:0000303|PubMed:22672125};
DE            EC=4.2.1.133 {ECO:0000269|PubMed:22672125};
DE   AltName: Full=8-hydroxy-copalyl diphosphate synthase {ECO:0000303|PubMed:22672125};
DE   Flags: Precursor;
GN   Name=CPS2 {ECO:0000303|PubMed:22672125};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND PATHWAY.
RX   PubMed=22672125; DOI=10.1111/j.1365-313x.2012.05068.x;
RA   Sallaud C., Giacalone C., Toepfer R., Goepfert S., Bakaher N., Roesti S.,
RA   Tissier A.;
RT   "Characterization of two genes for the biosynthesis of the labdane
RT   diterpene Z-abienol in tobacco (Nicotiana tabacum) glandular trichomes.";
RL   Plant J. 72:1-17(2012).
RN   [2]
RP   PATHWAY, AND REVIEW.
RX   PubMed=30468448; DOI=10.1039/c8np00077h;
RA   Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT   "Non-volatile natural products in plant glandular trichomes: chemistry,
RT   biological activities and biosynthesis.";
RL   Nat. Prod. Rep. 36:626-665(2019).
CC   -!- FUNCTION: Class-II terpene synthase that synthesizes 8-hydroxy-copalyl
CC       diphosphate. Involved in the biosynthesis of cis-abienol, a labdane
CC       diterpene that can be used as synthesis precursor of ambergris
CC       substitution fragance products. {ECO:0000269|PubMed:22672125}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + H2O = 8-
CC         hydroxycopalyl diphosphate; Xref=Rhea:RHEA:32703, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58756, ChEBI:CHEBI:64283; EC=4.2.1.133;
CC         Evidence={ECO:0000269|PubMed:22672125};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:22672125}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in the secretory cells of
CC       the glandular trichomes. {ECO:0000269|PubMed:22672125}.
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC       activity, presumably through binding to Mg(2+). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The expression of both CPS2 and ABS is necessary and
CC       sufficient to catalyze the biosynthesis of cis-abienol from
CC       geranylgeranyl diphosphate in a heterologous system.
CC       {ECO:0000305|PubMed:22672125}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; HE588139; CCD33018.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3CCC0; -.
DR   SMR; G3CCC0; -.
DR   BioCyc; MetaCyc:MON18C3-47; -.
DR   BRENDA; 4.2.1.133; 3645.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0102161; F:copal-8-ol diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR   GO; GO:1902243; P:copal-8-ol diphosphate(3-) biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
DR   GO; GO:1902247; P:geranylgeranyl diphosphate catabolic process; IDA:UniProtKB.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR001906; Terpene_synth_N.
DR   InterPro; IPR036965; Terpene_synth_N_sf.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SUPFAM; SSF48239; SSF48239; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..802
FT                   /note="Copal-8-ol diphosphate hydratase, chloroplastic"
FT                   /id="PRO_5000793116"
FT   MOTIF           382..385
FT                   /note="DXDD motif"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         382
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         384
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         468
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   802 AA;  93245 MW;  B20B8BA346E67D27 CRC64;
     MQVIITSSHR FFCHHLHQLK SPTSLSAQKA EFKKHGPRNW LFQTEGSLLY KPVRLNCATS
     DASYLGNVNE YLESDHSKNS EEKDIQVSRT IQMKGLTEEI KHMLNSMEDG RLNVLAYDTA
     WVSFIPNTTN NGNDQRPMFP SCLQWIIDNQ LSDGSWGEEI VFCIYDRLLN TLVCVIALTL
     WNTCLHKRNK GVMFIKENLS KLETGEVENM TSGFELVFPT LLEKAQQLDI DIPYDAPVLK
     DIYARREVKL TRIPKDVIHT IPTTVLFSLE GLRDDLDWQR LLKLQMPDGS FLISPASTAF
     AFMETNDEKC LAYLQNVVEK SNGGARQYPF DLVTRLWAID RLQRLGISYY FAEEFKELLN
     HVFRYWDEEN GIFSGRNSNV SDVDDTCMAI RLLRLHGYDV SPDALNNFKD GDQFVCFRGE
     VDGSPTHMFN LYRCSQVLFP GEKILEEAKN FTYNFLQQCL ANNRCLDKWV IAKDIPGEIW
     YALEFPWYAS LPRVEARYYI EQYGGADDIW IGKTLYRMPD VNNNVYLQAA KLDYNRCQSQ
     HRFEWLIMQE WFEKCNFQQF GISKKYLLVS YFLAAASIFE VEKSRERLAW AKSRIICKMI
     TSYYNDEATT WTTRNSLLME FKVSHDPTRK NGNETKEILV LKNLRQFLRQ LSEETFEDLG
     KDIHHQLQNA WETWLVFLRE EKNACQEETE LLVRTINLSG GYMTHDEILF DADYENLSNL
     TNKVCGKLNE LQNDKVTGGS KNTNIELDMQ ALVKLVFGNT SSNINQDIKQ TFFAVVKTFY
     YSAHVSEEIM NFHISKVLFQ QV
 
 
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