TPS3_PIPNI
ID TPS3_PIPNI Reviewed; 561 AA.
AC A0A2R4QKX7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Terpene synthase 3 {ECO:0000303|PubMed:29248443, ECO:0000303|Ref.1};
DE Short=PnTPS3 {ECO:0000303|PubMed:29248443, ECO:0000303|Ref.1};
DE AltName: Full=Copaene synthase {ECO:0000303|Ref.1};
DE Short=PnCop {ECO:0000303|PubMed:29248443};
DE EC=4.2.3.133 {ECO:0000269|PubMed:29248443};
DE AltName: Full=Germacrene D synthase {ECO:0000303|PubMed:29248443};
DE Short=PnGDS {ECO:0000303|PubMed:29248443};
DE EC=4.2.3.- {ECO:0000269|PubMed:29248443};
GN Name=TPS3 {ECO:0000303|PubMed:29248443, ECO:0000303|Ref.1};
OS Piper nigrum (Black pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Piperales; Piperaceae; Piper.
OX NCBI_TaxID=13216;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fruit;
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=29248443; DOI=10.1016/j.abb.2017.12.011;
RA Jin Z., Kwon M., Lee A.-R., Ro D.-K., Wungsintaweekul J., Kim S.-U.;
RT "Molecular cloning and functional characterization of three terpene
RT synthases from unripe fruit of black pepper (Piper nigrum).";
RL Arch. Biochem. Biophys. 638:35-40(2018).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds that contribute to the characteristic flavors of
CC black pepper (PubMed:29248443). Mediates the conversion of (2E,6E)-
CC farnesyl diphosphate (FPP) into alpha-copaene and germacrene D
CC (PubMed:29248443). {ECO:0000269|PubMed:29248443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene D;
CC Xref=Rhea:RHEA:68716, ChEBI:CHEBI:33019, ChEBI:CHEBI:49045,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68717;
CC Evidence={ECO:0000269|PubMed:29248443};
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:29248443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33992;
CC Evidence={ECO:0000269|PubMed:29248443};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.152 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:29248443};
CC Note=kcat is 0.185 sec(-1) with (2E,6E)-farnesyl diphosphate as
CC substrate. {ECO:0000269|PubMed:29248443};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:29248443}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems amd leaves, and, to a
CC lower extent, in roots and fruits. {ECO:0000269|PubMed:29248443}.
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|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; MF104556; AVY53326.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IDA:UniProtKB.
DR GO; GO:0052577; F:germacrene-D synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:1901931; P:alpha-copaene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic 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..561
FT /note="Terpene synthase 3"
FT /id="PRO_0000454953"
FT MOTIF 315..319
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 561 AA; 64520 MW; 48D906F1B3A7A02D CRC64;
MGFSFVTNAA IAAHMPPSKQ EIIRRDAKFH PTIWGDHFIQ YLDTPIDPPQ KVVERMEELK
KQVRAMLRDT NLDISLIDWI QRTGIAYHFE EQIAETLKHV YEASTLTTDS SKYLEHFDLR
HIALRFRLSR QQGYHASTDV FKRFMDEGDK FKQSIANDIE GMLSLYEASF MSVKGEAILD
EALAFTGKNL EATLPNLTGS LAQQVECALE IPLRRCTDLV KARRSISCYE NKNGRNEVVL
ELAKLDFNLL QAVHQRELAL LTSWWNELGA STNLPFTRNR VVELYFWVLE VLSKPEHARA
REIMVKSIIM ASILDDVYDV YGTLEELQLF TSALERWDLQ ALEQLPNTIK TAYSIVLRVF
KEYEDLLKPH EVYRVGFARK ALIPYMNAYF LEAKWFYSHH HPSFEEYMDN ALVSCGYPFL
FLVSLVGLDE IATKDVFEWA IKRPNIVVAA SMICRNRDDI VGHKEEQERG DVPSGVECYT
KDHGCTEEEA CMALQAMVDD AWKDINCELL HDTSMPKAIL MRAVGLARII SILYQYRDGY
SDSTHETKAH VTQVLVQPIP L
