ID   TPS5_PHYDL              Reviewed;         565 AA.
AC   J7LMP2;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Bicyclogermacrene synthase;
DE            EC=4.2.3.100;
DE   AltName: Full=Terpene synthase 5;
DE            Short=LdTPS5;
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       bicyclogermacrene as the major product. {ECO:0000269|PubMed:22867794}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = bicyclogermacrene +
CC         diphosphate; Xref=Rhea:RHEA:31999, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:63709, ChEBI:CHEBI:175763; EC=4.2.3.100;
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; JQ731633; AFR23369.1; -; mRNA.
DR   AlphaFoldDB; J7LMP2; -.
DR   SMR; J7LMP2; -.
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:1901934; P:bicyclogermacrene 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..565
FT                   /note="Bicyclogermacrene synthase"
FT                   /id="PRO_0000421952"
FT   MOTIF           317..321
FT                   /note="DDXXD motif"
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         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         461
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   565 AA;  66477 MW;  7FEBE5D4FDD4C3FB CRC64;
     MDLAKQISVV DSSLQDVTRN ITRPLANFHP NVWGDRFLLN NSDQVQLKMN ALDKEEAIEK
     LKEGVRRKLK EASNDYMRLI QMVDAIQRLG FAYHFEEEID QALQCLFERH HEYCKDNHDL
     YANSLSFRLL RQQGYRVSCE IFEKFKDVKG NFMLPNNGEV MGVLEFYEAT HLRVHGEDLL
     DHDFVLSREY LESVLPSLTN PLAEQVDHAL HQHSNRRGLS RLEARHYMPV YEQYASHDQY
     LLKLAKLDFN MLQSLHKEEL SELSRWWKGI DVARNLPYAR DRIVETYFWI LGVYFEPEYA
     AARKILVKVQ SLFSIIDDTF DAYGTFEELQ IFTQALERWS ISCLDQLPDY MKLIYKTVLE
     VYDEIEEEMI KQGTSYRTAY GIEAIKSLTR NYFMEAEWRE KKYTPTTDEH MRLALKTCGY
     TSLIIISFLG MGEVVKREAF DWVLSEPDFV KASLTINRLV DDIVGHEDEQ KRNHVVSSVE
     CYVQESKTSR EDAVYELNSR VESTWKDLNE GFLKPTKFPS PLLYRVLNYS RVIEVMYTKG
     DWYTNVGPEM QDYIRQLLID PVNVE