TPS8_PHYDL
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 03-AUG-2022, entry version 31.
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";
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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; -; 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; 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
