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 24-JAN-2024, entry version 47.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE588139; CCD33018.1; -; Genomic_DNA.
DR AlphaFoldDB; G3CCC0; -.
DR SMR; G3CCC0; -.
DR STRING; 4097.G3CCC0; -.
DR PaxDb; 4097-G3CCC0; -.
DR BioCyc; MetaCyc:MONOMER18C3-47; -.
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:1902247; P:geranylgeranyl diphosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.50.10.160; -; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR31739:SF30; COPAL-8-OL DIPHOSPHATE HYDRATASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR31739; ENT-COPALYL DIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF01397; Terpene_synth; 1.
DR SFLD; SFLDG01014; Terpene_Cyclase_Like_1_N-term; 1.
DR SFLD; SFLDG01605; Terpene_Cyclase_Like_1_N-term; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 2.
DR SUPFAM; SSF48576; Terpenoid synthases; 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
//
