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SBS_SOLHA
ID   SBS_SOLHA               Reviewed;         777 AA.
AC   B8XA41;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Santalene and bergamotene synthase, chloroplastic;
DE   AltName: Full=(+)-alpha-santalene synthase ((2Z,6Z)-farnesyl diphosphate cyclizing);
DE            EC=4.2.3.50;
DE   AltName: Full=(+)-endo-beta-bergamotene synthase ((2Z,6Z)-farnesyl diphosphate cyclizing);
DE            EC=4.2.3.53;
DE   AltName: Full=(-)-endo-alpha-bergamotene synthase ((2Z,6Z)-farnesyl diphosphate cyclizing);
DE            EC=4.2.3.54;
DE   Flags: Precursor;
GN   Name=SBS;
OS   Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=62890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RC   TISSUE=Trichome gland;
RX   PubMed=19155349; DOI=10.1105/tpc.107.057885;
RA   Sallaud C., Rontein D., Onillon S., Jabes F., Duffe P., Giacalone C.,
RA   Thoraval S., Escoffier C., Herbette G., Leonhardt N., Causse M.,
RA   Tissier A.;
RT   "A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl
RT   pyrophosphate in the wild tomato Solanum habrochaites.";
RL   Plant Cell 21:301-317(2009).
CC   -!- FUNCTION: (2Z,6Z)-farnesyl diphosphate cyclizing enzyme. Produces (+)-
CC       alpha-santalene, (+)-endo-beta-bergamotene, (-)-endo-alpha-bergamotene,
CC       and at lower amounts, (-)exo-alpha-bergamotene and (+)-epi-beta-
CC       santalene. Not able to use geranyl diphosphate, E,E-farnesyl
CC       diphosphate or E,E,E-geranylgeranyl diphosphate as substrates, but able
CC       to use Neryl diphosphate to make the monoterpene terpineol.
CC       {ECO:0000269|PubMed:19155349}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,6Z)-farnesyl diphosphate = (+)-alpha-santalene +
CC         diphosphate; Xref=Rhea:RHEA:30463, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:60374, ChEBI:CHEBI:61677; EC=4.2.3.50;
CC         Evidence={ECO:0000269|PubMed:19155349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,6Z)-farnesyl diphosphate = (+)-endo-beta-bergamotene +
CC         diphosphate; Xref=Rhea:RHEA:30467, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:60374, ChEBI:CHEBI:61678; EC=4.2.3.53;
CC         Evidence={ECO:0000269|PubMed:19155349};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,6Z)-farnesyl diphosphate = (1S,5S,6S)-alpha-bergamotene +
CC         diphosphate; Xref=Rhea:RHEA:30471, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:60374, ChEBI:CHEBI:61679; EC=4.2.3.54;
CC         Evidence={ECO:0000269|PubMed:19155349};
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:19155349}.
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. Tpse subfamily.
CC       {ECO:0000305}.
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DR   EMBL; FJ194970; ACJ38409.1; -; mRNA.
DR   AlphaFoldDB; B8XA41; -.
DR   SMR; B8XA41; -.
DR   PRIDE; B8XA41; -.
DR   KEGG; ag:ACJ38409; -.
DR   BioCyc; MetaCyc:MON-14819; -.
DR   BRENDA; 4.2.3.50; 3102.
DR   BRENDA; 4.2.3.53; 3102.
DR   BRENDA; 4.2.3.54; 3102.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0102062; F:alpha-santalene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102060; F:endo-alpha-bergamotene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102061; F:endo-beta-bergamotene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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   SUPFAM; SSF48239; SSF48239; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..777
FT                   /note="Santalene and bergamotene synthase, chloroplastic"
FT                   /id="PRO_0000405118"
FT   MOTIF           530..534
FT                   /note="DDXXD motif"
FT   BINDING         530
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         530
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         534
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         534
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   777 AA;  90626 MW;  AE19AD4DA742979D CRC64;
     MIVGYRSTII TLSHPKLGNG KTISSNAIFQ RSCRVRCSHS TPSSMNGFED ARDRIRESFG
     KVELSPSSYD TAWVAMVPSK HSLNEPCFPQ CLDWIIENQR EDGSWGLNPS HPLLLKDSLS
     STLACLLALT KWRVGDEQIK RGLGFIETQS WAIDNKDQIS PLGFEIIFPS MIKSAEKLNL
     NLAINKRDST IKRALQNEFT RNIEYMSEGV GELCDWKEII KLHQRQNGSL FDSPATTAAA
     LIYHQHDKKC YEYLNSILQQ HKNWVPTMYP TKIHSLLCLV DTLQNLGVHR HFKSEIKKAL
     DEIYRLWQQK NEQIFSNVTH CAMAFRLLRM SYYDVSSDEL AEFVDEEHFF AISGKYTSHV
     EILELHKASQ LAIDHEKDDI LDKINNWTRT FMEQKLLNNG FIDRMSKKEV ELALRKFYTI
     SDLAENRRCI KSYEENNFKI LKAAYRSPNI YNKDLFIFSI RNFELCQAQH QEELQQFKRW
     FEDYRLDQLG IAERYIHDTY LCAVIVVPEP ELSDARLLYA KYVLLLTIVD DQFDSFASTD
     ECLNIIELVE RWDDYASVGY KSEKVKVFFS TLYKSIEELV TIAEIKQGRS VKNHLLNLWL
     ELVKLMLMER VEWFSGKTIP SIEEYLYVTS ITFGARLIPL TTQYFLGIKI SEDILESDEI
     YGLCNCTGRV LRILNDLQDS KKEQKEDSVT IVTLLMKSMS EEEAIMKIKE ILEMNRRELL
     KMVLVQKKGS QLPQICKDIF WRTSNWADFI YLQTDGYRIA EEMKNHIDEV FYKPLNH
 
 
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