TPS2_PIPNI
ID TPS2_PIPNI Reviewed; 562 AA.
AC A0A1V0E4A6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Terpene synthase 2 {ECO:0000303|PubMed:29248443};
DE Short=PnTPS2 {ECO:0000303|PubMed:29248443};
DE AltName: Full=Cadinene synthase {ECO:0000303|PubMed:29248443};
DE Short=PnCDS {ECO:0000303|PubMed:29248443};
DE EC=4.2.3.- {ECO:0000269|PubMed:29248443};
DE AltName: Full=Cadinol synthase {ECO:0000303|PubMed:29248443};
DE Short=PnCO {ECO:0000303|PubMed:29248443};
DE EC=4.2.3.- {ECO:0000269|PubMed:29248443};
GN Name=TPS2 {ECO:0000303|PubMed:29248443};
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND 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-cadinene, delta-cadinene and
CC delta-cadinol (PubMed:29248443). {ECO:0000269|PubMed:29248443}.
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:29248443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557;
CC Evidence={ECO:0000269|PubMed:29248443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-cadinene + diphosphate;
CC Xref=Rhea:RHEA:69444, ChEBI:CHEBI:33019, ChEBI:CHEBI:80749,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:29248443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69445;
CC Evidence={ECO:0000269|PubMed:29248443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = delta-cadinol +
CC diphosphate; Xref=Rhea:RHEA:69448, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:156223, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000269|PubMed:29248443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69449;
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=18.4 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:29248443};
CC Note=kcat is 0.694 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: Expressed at low levels in stems, leaves, roots and
CC 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; KU953958; ARB08606.1; -; mRNA.
DR BRENDA; 4.2.3.13; 4863.
DR UniPathway; UPA00213; -.
DR GO; GO:0047461; F:(+)-delta-cadinene 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:1901928; P:cadinene 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..562
FT /note="Terpene synthase 2"
FT /id="PRO_0000454952"
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 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 562 AA; 64564 MW; 446D074AA937800B CRC64;
MDAVSCAINA LSAQAPPKHL GGNNVGRKSV TFPKDIWGDY FLKISPNEEK LDSWRVRAKE
LKEKVFDILS CAKGAEQVHI IDALYHLGVS YQFEKEIEEA LKNMLTTYND DTSTEDDLYT
LALRFRLLRQ NGFHASTKAL NKFKDAHGSF REDLASDVMG LLSLYEASYA GTVDDLILDE
ALAFTKIHLK AALPHLDSHL AQRVSHSLEL PLHKRIQRLE AREFISLCEK DDSIVIKELL
EFAKLDYNIL QALHQWELKE LTKWWKKLNL VGKMTFARDR MTEIYFYVSG FFFEPQYSRG
RIISSKILAI CSVVDDEYDV YGTLDELQVF TDAICRLDVA AMENLPEYVK PLYEAIFFSL
KEFEEELARE GNAYRVNYLR EEVKNLCKSY LQETKWLHQR YIPTLEEYLL VSEISSTYTV
IFNGCFVGCG EIATKEVFEW FQAFPKLLSD SARIGRIADD IMSCKFEQSR GHCPSAVECC
MEEHQCTKEV ALGNLDGVLG RAWKDMNKAC MRPTPFPMEV LRPIVNLARM AEISYQYEDG
YTFSGGKTKE RISMLYKDPI PV
