TPS7_PHYDL
ID TPS7_PHYDL Reviewed; 542 AA.
AC J7LQ09;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Trans-alpha-bergamotene synthase;
DE EC=4.2.3.81;
DE AltName: Full=Terpene synthase 7;
DE Short=LdTPS7;
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 trans-alpha-bergamotene as the major product.
CC {ECO:0000269|PubMed:22867794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene +
CC diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62756, ChEBI:CHEBI:175763; EC=4.2.3.81;
CC 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; JQ731635; AFR23371.1; -; mRNA.
DR AlphaFoldDB; J7LQ09; -.
DR SMR; J7LQ09; -.
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:1901940; P:(-)-exo-alpha-bergamotene 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..542
FT /note="Trans-alpha-bergamotene synthase"
FT /id="PRO_0000421954"
FT MOTIF 295..299
FT /note="DDXXD motif"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 542 AA; 63549 MW; 52B0810FD049261B CRC64;
MEARRSGNFK ASIWDDDFLQ SLTSPYTAKE YLKQADKLKW QVKVIIKETK QRLDQLDLID
NIQRLGISHH FRDEIQRVLQ NIYEKMRVEC PDRMLMEKDL YSTSLQFRLL RQHGYHVSQD
VFCSFMDGAG NFQAVDDLKG ILALYEASFL SREGENILGS ARDFSTRHLK QKLEEITDPI
LAEKIRRALE LPLHWRLQKL EAIWFINIYE SRFDANLILL QLAKLEFNMV QAQYQEDLKW
LSRWYKETGL PEKMNFARDR LAECFLWALG FIPEAHLGQA RKILTKIAVL IVIMDDFYDI
YGTLDEIKVF TEELQRWDIN ALDNLPEYMR ICFLAIFNTA NEIAYDILRD QGINIISNLR
RLWAELGRVY YTEAKWYHSG YFPSTEEYLN VAWISITGPV LLFHAYFSIM NPIDMKELQY
LEQYPGIIRW PSTVLRLADD LGTASDEIKR GDVPKSIQCY MHETGCSEEE AREYVKQLID
TTLKKMNKEI LMEKPTNDFG ATAMNLARIS LFFYQYGDGF GVPHNQTKEN LVSLIVKPIC
LT
