ID   SPIBS_SANSP             Reviewed;         576 AA.
AC   E3W206;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Alpha-bisabolol synthase;
DE            Short=SspiBS;
DE            EC=4.2.3.-;
OS   Santalum spicatum (Australian sandalwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Santalales; Santalaceae; Santalum.
OX   NCBI_TaxID=453088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=21454632; DOI=10.1074/jbc.m111.231787;
RA   Jones C.G., Moniodis J., Zulak K.G., Scaffidi A., Plummer J.A.,
RA   Ghisalberti E.L., Barbour E.L., Bohlmann J.;
RT   "Sandalwood fragrance biosynthesis involves sesquiterpene synthases of both
RT   the terpene synthase (TPS)-a and TPS-b Subfamilies, including santalene
RT   synthases.";
RL   J. Biol. Chem. 286:17445-17454(2011).
CC   -!- FUNCTION: Produces a mixture of beta-bisabolene and alpha-bisabolol,
CC       along with traces of alpha-bisabolene and farnesene isomers from
CC       (2E,6E)-farnesyl diphosphate in fragrance biosynthesis.
CC       {ECO:0000269|PubMed:21454632}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; HQ343280; ADO87004.1; -; mRNA.
DR   AlphaFoldDB; E3W206; -.
DR   SMR; E3W206; -.
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   2: Evidence at transcript level;
KW   Lyase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..576
FT                   /note="Alpha-bisabolol synthase"
FT                   /id="PRO_0000418946"
FT   MOTIF           323..327
FT                   /note="DDXXD motif"
FT   BINDING         323
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         477
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   576 AA;  65775 MW;  EC906DAEF3DE7C2B CRC64;
     MDAFATSPTT ALFETVNCNA HVAPMAGEDS SENRPASNYK PSTWDYEFLQ SLATTNNTVG
     EKHTRMADKL KEEVKSMMKG TMEPVAKLEL INIVQRLGLK YRFESEIKEE LFSLYKDGTD
     AWWVGNLHAT ALRFRLLREN GIFVPQDVFE TFKDKSGEFK SQLCKDVRGL LSLYEASYLG
     WEGEELLDEA KKFSTTNLNN VKESISSNTL GRLVKHALNL PLHWSAARYE ARWFIDEYER
     EENVIPNLLK YAKLDFNVVQ SIHQKELGNL ARWWVETGLD KLGFVRNTLM QNFMWGCAMA
     FEPQYGKVRD AAVKLGSLIT MVDDVYDVYG TLEELEIFTD IVDRWDINGI DKLPRNISMI
     VLTMFNTANQ ISYDLLRDRG FNSIPHIAEA WATLCKTYLK EAKWYHSGYK PTLEEYLENG
     LVSISFVLSL VTAYLQTERL ENLTYESAAY VNSVPPLVRY SGLLNRLYND LGTSSAEIAR
     GDTLKSIQCY MTQTGATEEV AREHIKGLVH EAWKGMNRCL FEQTPLAEPF VGFNVNTVRG
     SQFFYQHGDG YAVTESWTKD LSLSVLIHPI PLNEED