CLDS_CISCR
ID CLDS_CISCR Reviewed; 808 AA.
AC E2IHE0;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Copal-8-ol diphosphate hydratase, chloroplastic {ECO:0000303|PubMed:20595348};
DE EC=4.2.1.133 {ECO:0000269|PubMed:20595348};
DE AltName: Full=Copal-8-ol diphosphate synthase {ECO:0000303|PubMed:20595348};
DE Short=CcCLS {ECO:0000303|PubMed:20595348};
DE Flags: Precursor;
GN Name=CLS {ECO:0000303|PubMed:20595348};
OS Cistus creticus subsp. creticus (Rock rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Cistaceae; Cistus.
OX NCBI_TaxID=483148;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION BY WOUNDING, AND PATHWAY.
RX PubMed=20595348; DOI=10.1104/pp.110.159566;
RA Falara V., Pichersky E., Kanellis A.K.;
RT "A copal-8-ol diphosphate synthase from the angiosperm Cistus creticus
RT subsp. creticus is a putative key enzyme for the formation of
RT pharmacologically active, oxygen-containing labdane-type diterpenes.";
RL Plant Physiol. 154:301-310(2010).
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: Involved in the biosynthesis of oxygen-containing labdane-
CC type diterpenes that may be implicated in direct and indirect defense
CC mechanisms. No activity with geranyl diphosphate or farnesyl
CC diphosphate as substrate. {ECO:0000269|PubMed:20595348}.
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:20595348};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:20595348}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves and trichomes. Not
CC detected in roots and seeds. Higher expression in young leaves than in
CC fully expanded leaves. {ECO:0000269|PubMed:20595348}.
CC -!- INDUCTION: Up-regulated by wounding. {ECO:0000269|PubMed:20595348}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; HM537017; ADJ93862.1; -; mRNA.
DR AlphaFoldDB; E2IHE0; -.
DR SMR; E2IHE0; -.
DR KEGG; ag:ADJ93862; -.
DR BRENDA; 4.2.1.133; 10165.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102161; F:copal-8-ol diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR GO; GO:0033385; P:geranylgeranyl diphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Coiled coil; Lyase; Magnesium; Metal-binding; Plant defense;
KW Plastid; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..808
FT /note="Copal-8-ol diphosphate hydratase, chloroplastic"
FT /id="PRO_0000419748"
FT COILED 190..219
FT /evidence="ECO:0000255"
FT MOTIF 391..394
FT /note="DXDD motif"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 393
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
SQ SEQUENCE 808 AA; 92655 MW; 2F3C41898B054B11 CRC64;
MAFTFTSAHL FLPVTENHSV HVNYSIPPGN WRLWSTAKGG SNKLDIRRLR CSARRTPEPL
AQGSNGGRDG VEAIQRLQTI ADDKIDGGAN ELGIVVWDLI RDGVDAVKSM FDSMGDGDIS
ISAYDTAWVA LVKDVNGSGG PQFPSSLQWI VDNQLPDGSW GDSEVFSAYD RLLKTLACVV
ALKSWNIRPD KCQKGLKFFR DNISKLEKEN VEASAQMLSG FEVVFLSLIE VARRLDIQIP
LHSPVFEDLI ARRNLKFAKI PLDLMHNVPT SLLNSLEGMT GVELDWEKLL KLQSQDGSFI
TSPSSTAFAL MQTNDTKCLG YLKFVVQKFN GGAPGQYPVE IFERIWVVDR LQRLGISRYF
QLEIKECCLD YAFKHWTQYG SSWARNTPVY DLDDTCMAFR ILRLHGYDVS AEAFRHFEKN
GVFFCFGWET TQSVTVNFNL YRATQVAFPG ENILKEAKQF SFNFLMKKQA AREFQDKWVI
LKDFPGELKY ALEFPWYASL PRVETRFYVE QYGGDNDVWI GKTLYRMPYI NNNVYLELAK
LDFNNCQALH RKEWETMQKW FMESKLDEFG VSSKTLLESY FLAAASIFEP ERSTERLAWA
KTAFLMETIG SYFDDEMNSK DLRKAFVQEF KNIYERRMEA KGTKWNLIII LLTTLNHLTE
VCGRDINSYL CHSWEKWMMM WEPEGDRYKG AAELLSNSIN LSSGRLFSND TLSHPNYEKL
VTLSNKLCHQ LGNSRRGNHN EDSDIKDTKI EIAMQELVQL VHQNSSDDIS MDLKQTFFAV
VRSFYYAAHC DRGTINSHIV KVLFESVV
