CADS_LAVAN
ID CADS_LAVAN Reviewed; 555 AA.
AC U3LW50;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Tau-cadinol synthase {ECO:0000303|PubMed:24078339};
DE Short=LaCADS {ECO:0000303|PubMed:24078339};
DE EC=4.2.3.173 {ECO:0000269|PubMed:24078339};
DE AltName: Full=(+)-gamma-cadinene synthase {ECO:0000305};
DE AltName: Full=Gamma-cadinene synthase {ECO:0000305};
DE EC=4.2.3.92 {ECO:0000269|PubMed:24078339};
GN Name=CADS {ECO:0000303|PubMed:24078339};
OS Lavandula angustifolia (Lavender).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Lavandulinae;
OC Lavandula.
OX NCBI_TaxID=39329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF ASP-532 AND ASP-533.
RX PubMed=24078339; DOI=10.1007/s11103-013-0131-3;
RA Jullien F., Moja S., Bony A., Legrand S., Petit C., Benabdelkader T.,
RA Poirot K., Fiorucci S., Guitton Y., Nicole F., Baudino S., Magnard J.L.;
RT "Isolation and functional characterization of a tau-cadinol synthase, a new
RT sesquiterpene synthase from Lavandula angustifolia.";
RL Plant Mol. Biol. 84:227-241(2014).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC sesquiterpenes and sesquiterpenoid alcohols (PubMed:24078339). Converts
CC farnesyl diphosphate (FPP) to tau-cadinol (PubMed:24078339). Converts
CC FPP to gamma-cadinene (PubMed:24078339). Tau-cadinol is the major
CC product (PubMed:24078339). {ECO:0000269|PubMed:24078339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + tau-
CC cadinol; Xref=Rhea:RHEA:54052, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138042, ChEBI:CHEBI:175763; EC=4.2.3.173;
CC Evidence={ECO:0000269|PubMed:24078339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54053;
CC Evidence={ECO:0000269|PubMed:24078339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-gamma-cadinene +
CC diphosphate; Xref=Rhea:RHEA:31827, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:63205, ChEBI:CHEBI:175763; EC=4.2.3.92;
CC Evidence={ECO:0000269|PubMed:24078339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31828;
CC Evidence={ECO:0000269|PubMed:24078339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JX401282; AGL98418.1; -; mRNA.
DR AlphaFoldDB; U3LW50; -.
DR SMR; U3LW50; -.
DR KEGG; ag:AGL98418; -.
DR BRENDA; 4.2.3.173; 9723.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..555
FT /note="Tau-cadinol synthase"
FT /id="PRO_0000452461"
FT MOTIF 307..311
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 270
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 448
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 451
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT MUTAGEN 532
FT /note="D->G: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:24078339"
FT MUTAGEN 533
FT /note="D->G: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:24078339"
SQ SEQUENCE 555 AA; 64576 MW; D711D598F5C83813 CRC64;
MATSAVVNCL GGVRPHTIRY EPNMWTHTFS NFSIDEQVQG EYAEEIEALK QEVRSMLTAA
TTCKEQLILI DTLERLGLSY HFETEIEQKL KEIILHINRE EDASGGDCDL YTTSLGFRVI
RQHQYHISCG VFEKYLDKDG KFEESLSSDT EGILSLYEAA HVRFRDETLL QEAARFSRHH
LKGMEEVLES PLREKVQRAL QHPLHRDIPI FYAHFFISNI YQKDDSRNEL LLKLAKSNFM
FLQNLYKEEL SQLSRWWNKF DLKSKLPYAR DRLVEAYIWG VGYHYEPRYA YVRRGLVIGI
QIIAIMDDTY DNYATVDEAQ LFTEMFERWS MDGIDGVPDY LKIAYHFVVS AFEDYERDAG
KLGKQFAAPY FKQTIQQLAR AYNQELKWVM GTQSMPSFQD YAKNSEITSC IYIMSASVFH
GLESVTQETI DWLKNEPNFA VSTGMIGRYW DDIGSHERES RGGKMLTAVG CYMKQYGVSK
KEAVRKFREQ VEDLWKDVNK GYTAMTCMPR ETAVLFLNYA RMCDASYTEN NDDGYTDPDF
SKRKISALFL DPLVF
