ID   TPS6_PHYDL              Reviewed;         555 AA.
AC   J7LJN5;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Beta-caryophyllene synthase;
DE            EC=4.2.3.-;
DE   AltName: Full=Terpene synthase 6;
DE            Short=LdTPS6;
OS   Phyla dulcis (Aztec sweet herb) (Lippia dulcis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Verbenaceae; Lantaneae; Phyla.
OX   NCBI_TaxID=542674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22867794; DOI=10.1016/j.abb.2012.07.010;
RA   Attia M., Kim S.U., Ro D.K.;
RT   "Molecular cloning and characterization of (+)-epi-alpha-bisabolol
RT   synthase, catalyzing the first step in the biosynthesis of the natural
RT   sweetener, hernandulcin, in Lippia dulcis.";
RL   Arch. Biochem. Biophys. 527:37-44(2012).
CC   -!- FUNCTION: Sesquiterpene synthase converting farnesyl diphosphate to
CC       beta-caryophyllene as the major product. {ECO:0000269|PubMed:22867794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (+)-(E)-beta-caryophyllene +
CC         diphosphate; Xref=Rhea:RHEA:31815, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:63190, ChEBI:CHEBI:175763;
CC         Evidence={ECO:0000269|PubMed:22867794};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; JQ731634; AFR23370.1; -; mRNA.
DR   AlphaFoldDB; J7LJN5; -.
DR   SMR; J7LJN5; -.
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:1901937; P:beta-caryophyllene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0045339; P:farnesyl diphosphate catabolic 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="Beta-caryophyllene synthase"
FT                   /id="PRO_0000421953"
FT   MOTIF           313..317
FT                   /note="DDXXD motif"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  63876 MW;  B4D8D698E7C04410 CRC64;
     MGIHSSAENV ALENVRQSVT YHPSVWGDYF LTPASNHEES STSEGEELQE SRQEVEKLLG
     ATHDDSLQKL ELIDAIQRLG VDHHFQKEIE KSLQDIYLRC CNDKDDYDHN QTDLHTVALR
     FRLLRQQGYN ISSETFNKFT DRNGKFEESL ADDVRGMLSL YEAAHCGVQG EKILDEALVF
     SSSNLKSILA KNHMSNSGLT ARIEEAFDTP IRKCLTNFGA RKFMSMYEED ESHSEALLKF
     ARLDFNFSQK LHQKEISDLT RWWKELDFKT KLPFARDRMV ECYCWTLGIH PEPQYNLARN
     FLSKVIMLAS VIDDIYDVRG TLDELQLFTD AIQRWDISAM EQLPPYMRVC YEALLNVYAE
     VEELERIDGP YRVHYAKEEM KKLARAYLEE SQWLYKKYIP TFKEYMSVAI PSSGYIMVAG
     NCLVGLGNSL VMKDFDWVSC EPLMVKASAI IARLMDDMAG HGFEKKISAV ECYTNENGAS
     EKEAFEELEK QVSNAWKDMN QEFLHPTAVS MTVLTRVLNA ARVIHLLYKD GDSYTNSKTY
     IKELIEAVLI QPVKI