ID TPS8_PHYDL Reviewed; 546 AA. AC J7LH11; DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2012, sequence version 1. DT 27-MAR-2024, entry version 34. DE RecName: Full=(+)-epi-alpha-bisabolol synthase; DE EC=4.2.3.138; DE AltName: Full=Terpene synthase 8; DE Short=LdTPS8; 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, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. 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 involved in the biosynthesis of (+)- CC epi-alpha-bisabolol, a precursor of the natural sweetner hernandulcin. CC {ECO:0000269|PubMed:22867794}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-epi-alpha-bisabolol + CC diphosphate; Xref=Rhea:RHEA:34503, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:68658, ChEBI:CHEBI:175763; CC EC=4.2.3.138; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.8 uM for (2E,6E)-farnesyl diphosphate CC {ECO:0000269|PubMed:22867794}; CC Note=kcat is 0.04 sec(-1) for (2E,6E)-farnesyl diphosphate.; 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}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The taste of sweet - Issue CC 148 of May 2013; CC URL="https://web.expasy.org/spotlight/back_issues/148"; 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; JQ731636; AFR23372.1; -; mRNA. DR AlphaFoldDB; J7LH11; -. DR SMR; J7LH11; -. DR KEGG; ag:AFR23372; -. DR BRENDA; 4.2.3.138; 13174. 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:1901943; P:(+)-epi-alpha-bisabolol 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; 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; 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 PANTHER; PTHR31225:SF9; 1,8-CINEOLE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. PE 1: Evidence at protein level; KW Lyase; Magnesium; Metal-binding. FT CHAIN 1..546 FT /note="(+)-epi-alpha-bisabolol synthase" FT /id="PRO_0000421955" FT MOTIF 297..301 FT /note="DDXXD motif" FT BINDING 297 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 297 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 301 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 301 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 441 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 445 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 449 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000250" SQ SEQUENCE 546 AA; 63782 MW; DE64E5D3475494B5 CRC64; MNSTSRRSAN YKPTIWNNEY LQSLNSIYGE KRFLEQAEKL KDEVRMLLEK TSDPLDHIEL VDVLQRLAIS YHFTEYIDRN LKNIYDILID GRRWNHADNL HATTLSFRLL RQHGYQVSPE VFRNFMDETG NFKKNLCDDI KGLLSLYEAS YLLTEGETIM DSAQAFATHH LKQKLEENMN KNLGDEIAHA LELPLHWRVP KLDVRWSIDA YERRQDMNPL LLELAKLDFN IAQSMYQDEL KELSRWYSKT HLPEKLAFAR DRLVESYLWG LGLASEPHHK YCRMMVAQST TLISIIDDIY DVYGTLDELQ LFTHAVDRWD IKYLEQLPEY MQICFLALFN TVNERSYDFL LDKGFNVIPH SSYRWAELCK TYLIEANWYH SGYKPSLNEY LNQGLISVAG PHALSHTYLC MTDSLKEKHI LDLRTNPPVI KWVSILVRLA DDLGTSTDEL KRGDNPKSIQ CHMHDTGCNE EETRAYIKNL IGSTWKKINK DVLMNFEYSM DFRTAAMNGA RVSQFMYQYD DDGHGVPEGK SKERVCSLIV EPIPLP //