TPS1_PHYDL
ID TPS1_PHYDL Reviewed; 564 AA.
AC J7LP58;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Bifunctional sesquiterpene synthase 1;
DE AltName: Full=Alpha-copaene synthase;
DE EC=4.2.3.133;
DE AltName: Full=Delta-cadinene synthase;
DE EC=4.2.3.-;
DE AltName: Full=Terpene synthase 1;
DE Short=LdTPS1;
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, AND CATALYTIC ACTIVITY.
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 converting farnesyl diphosphate to
CC alpha copaene and delta-cadinene as the major products.
CC {ECO:0000269|PubMed:22867794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate;
CC Xref=Rhea:RHEA:33991, ChEBI:CHEBI:10221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.133;
CC Evidence={ECO:0000269|PubMed:22867794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate;
CC Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564,
CC ChEBI:CHEBI:175763; 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 -!- 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}.
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DR EMBL; JQ731632; AFR23368.1; -; mRNA.
DR AlphaFoldDB; J7LP58; -.
DR SMR; J7LP58; -.
DR BRENDA; 4.2.3.13; 13174.
DR BRENDA; 4.2.3.133; 13174.
DR UniPathway; UPA00213; -.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:1901931; P:alpha-copaene biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901928; P:cadinene 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..564
FT /note="Bifunctional sesquiterpene synthase 1"
FT /id="PRO_0000421951"
FT MOTIF 317..321
FT /note="DDXXD motif"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 564 AA; 65602 MW; 0E49109A2AA56DBC CRC64;
MALAKESSIV VSSSPDVTHN ITRPVASYHP NVWGDRFLLS SSDQVQLTMK ARDDKVVVDE
LKKEVRRKLK EASNDYIRLL QTVDVIQRLG LAYHFEEEID QALRYLFETF HDYSEDSQDM
YANSLSFRLL RQHGYRISCE IFEKFKDANG GFKIPNIEGV MGMLEFYEAT HLRVRGEDIL
DHGFVFSRNY LKSVLPSLSN PLAAQVDRAL NQNSNRRGLP RLEARHFMSV YEQYASHDQA
LLKLAKLNFN ILQSLHKVEL SEISRWWKGV DIARNFPYAR DRIVELYFWV LGVYFEPQYA
VGRKITTKVI AIASLLDDTF DAYGTFEELR IFAEAVERWS VSCLDQLPEY MKLLYKTMLE
VSDEIEEEMT KLGTPFRIAY GIEAIKTFAR SYFLEAKWRE EKYKPTTEEY MGLATKTCGY
KSLIITSFLA MGDIPKREHF DWVLSDPDFV MASCIICRLA DDIVGHEFEQ TRDHIPSSVE
CYTQEHKTSK EDAVNELYDR LESAWKDLNE GFLRPTKIPA ALLYRVLNYC RIIEVMYSRG
DWYTHVGPEM QGFVRQLLVD PVPE
