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 27-MAR-2024, entry version 51. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FJ194970; ACJ38409.1; -; mRNA. DR AlphaFoldDB; B8XA41; -. DR SMR; B8XA41; -. DR KEGG; ag:ACJ38409; -. DR BioCyc; MetaCyc:MONOMER-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 GO; GO:0006629; P:lipid metabolic process; IEA:UniProt. DR Gene3D; 1.50.10.160; -; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 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 PANTHER; PTHR31739:SF33; BETA-PHELLANDRENE SYNTHASE (NERYL-DIPHOSPHATE-CYCLIZING), CHLOROPLASTIC; 1. DR PANTHER; PTHR31739; ENT-COPALYL DIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. DR SFLD; SFLDG01014; Terpene_Cyclase_Like_1_N-term; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 2. DR SUPFAM; SSF48576; Terpenoid synthases; 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 //