CARS_TANPA
ID CARS_TANPA Reviewed; 548 AA.
AC F8UL81;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=E-beta-caryophyllene synthase {ECO:0000303|PubMed:21620424};
DE Short=TpCarS {ECO:0000303|PubMed:21620424};
DE EC=4.2.3.57 {ECO:0000269|PubMed:21620424};
GN Name=CarS {ECO:0000303|PubMed:21620424};
OS Tanacetum parthenium (Feverfew) (Matricaria parthenium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Anthemidinae; Tanacetum.
OX NCBI_TaxID=127999;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21620424; DOI=10.1016/j.phytochem.2011.04.021;
RA Majdi M., Liu Q., Karimzadeh G., Malboobi M.A., Beekwilder J., Cankar K.,
RA de Vos R., Todorovic S., Simonovic A., Bouwmeester H.;
RT "Biosynthesis and localization of parthenolide in glandular trichomes of
RT feverfew (Tanacetum parthenium L. Schulz Bip.).";
RL Phytochemistry 72:1739-1750(2011).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of beta-
CC caryophyllene, a sesquiterpene with anti-inflammatory and anti-
CC carcinogenic activities. {ECO:0000269|PubMed:21620424}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:21620424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:21620424};
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:0000269|PubMed:21620424}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- TISSUE SPECIFICITY: Higher levels in leaves than in flowers and stems.
CC {ECO:0000269|PubMed:21620424}.
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:0000250|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JF819849; AEH41845.1; -; mRNA.
DR AlphaFoldDB; F8UL81; -.
DR SMR; F8UL81; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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..548
FT /note="E-beta-caryophyllene synthase"
FT /id="PRO_0000448395"
FT MOTIF 301..305
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 548 AA; 63519 MW; 62290CE167959605 CRC64;
MSAKEEKVIR PIVHFPPSVW ADQFLIFDDE QAEQANVEQV VNELREDVRK DIVSSLDVQA
EHTNLLKLID AIQRLGIAYY FEGEIEQALQ HIYDTYGDDW KGRSPSLWFR IFRQQGFYVS
CDIFKNYKEE DGSFKESLTN DVEGLLELYE ATYLGVQGEG ILDDALVFTR TCLDKLAKDL
VHSNPTLSTH IQEALQQPLH KRLTRLEALR YIPTYEQLSS HNESLLKLAK LGFNLLQSLH
RKELSEVSRW WKGLDIPNNL PYARDRMVEC YFWALGVYFE PKYSRARIFL AKVISLATVL
DDTYDAYGIY EELKIFTEAI QRWSITCIDT LPEYMKLLYK GVLNIYKEME EIMGKEGKAH
HLSYAKESMK EFIRSYMMEA KWANEGYVPT AEEHMSVAFV SSGYSMLATT CFVGMGDIVT
DEAFEWALTK PPIVKASCAI ARLMDDIHSQ KEEKERIHVA SSVESYMKQY DVTEEHVHKV
FHKKIEDAWK DITRESPVCK DIPMPLMTRV INLARVMDVL YKHKDGFTNV GQELKDHIKS
LLVHPIPI
