ID   BISS_ZINOF              Reviewed;         550 AA.
AC   D2YZP9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=(S)-beta-bisabolene synthase;
DE            EC=4.2.3.55;
DE   AltName: Full=Terpene synthase 1;
DE            Short=ZoTPS1;
GN   Name=TPS1;
OS   Zingiber officinale (Ginger) (Amomum zingiber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Zingiberaceae;
OC   Zingiber.
OX   NCBI_TaxID=94328;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Kintoki;
RX   PubMed=20229191; DOI=10.1007/s00425-010-1137-6;
RA   Fujisawa M., Harada H., Kenmoku H., Mizutani S., Misawa N.;
RT   "Cloning and characterization of a novel gene that encodes (S)-beta-
RT   bisabolene synthase from ginger, Zingiber officinale.";
RL   Planta 232:121-130(2010).
CC   -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC       bisabolene. {ECO:0000269|PubMed:20229191}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (S)-beta-bisabolene +
CC         diphosphate; Xref=Rhea:RHEA:28266, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:49263, ChEBI:CHEBI:175763; EC=4.2.3.55;
CC         Evidence={ECO:0000269|PubMed:20229191};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- TISSUE SPECIFICITY: Expressed only in young rhizomes. Not detected in
CC       leaves, roots and mature rhizomes. {ECO:0000269|PubMed:20229191}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB511914; BAI67934.1; -; mRNA.
DR   AlphaFoldDB; D2YZP9; -.
DR   SMR; D2YZP9; -.
DR   KEGG; ag:BAI67934; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; Manganese; Metal-binding.
FT   CHAIN           1..550
FT                   /note="(S)-beta-bisabolene synthase"
FT                   /id="PRO_0000412109"
FT   MOTIF           303..307
FT                   /note="DDXXD motif"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         455
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  64431 MW;  A86BC830D4B4D0AE CRC64;
     MELVDTPSLE VFEDVVVDRQ VAGFDPSFWG DYFITNQKSQ SEAWMNERAE ELKNEVRSMF
     QNVTGILQTM NLIDTIQLLG LDYHFMEEIA KALDHLKDVD MSKYGLYEVA LHFRLLRQKG
     FNISSDVFKK YKDKEGKFME ELKDDAKGLL SLYNAAYFGT KEETILDEAI SFTKDNLTSL
     LKDLNPPFAK LVSLTLKTPI QRSMKRIFTR SYISIYQDEP TLNETILELA KLDFNMLQCL
     HQKELKKICA WWNNLNLDIM HLNFIRDRVV ECYCWSMVIR HEPSCSRARL ISTKLLMLIT
     VLDDTYDSYS TLEESRLLTD AIQRWNPNEV DQLPEYLRDF FLKMLNIFQE FENELAPEEK
     FRILYLKEEW KIQSQSYFKE CQWRDDNYVP KLEEHMRLSI ISVGFVLFYC GFLSGMEEAV
     ATKDAFEWFA SFPKIIEACA TIIRITNDIT SMEREQKRAH VASTVDCYMK EYGTSKDVAC
     EKLLGFVEDA WKTINEELLT ETGLSREVIE LSFHSAQTTE FVYKHVDAFT EPNTTMKENI
     FSLLVHPIPI