TPS1_PIPNI
ID TPS1_PIPNI Reviewed; 559 AA.
AC A0A1V0E492;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Terpene synthase 1 {ECO:0000303|PubMed:29248443};
DE Short=PnTPS1 {ECO:0000303|PubMed:29248443};
DE AltName: Full=Alpha-humulene synthase {ECO:0000303|PubMed:29248443};
DE EC=4.2.3.104 {ECO:0000269|PubMed:29248443};
DE AltName: Full=Beta-caryophyllene synthase {ECO:0000303|PubMed:29248443};
DE Short=PnCPS {ECO:0000303|PubMed:29248443};
DE EC=4.2.3.57 {ECO:0000269|PubMed:29248443};
GN Name=TPS1 {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 beta-caryophyllene and, as a minor
CC compound, into alpha-humulene (PubMed:29248443).
CC {ECO:0000269|PubMed:29248443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:29248443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:29248443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.104;
CC Evidence={ECO:0000269|PubMed:29248443};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896;
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=21 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:29248443};
CC Note=kcat is 0.455 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 and, to a lower extent,
CC in leaves, 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; KU953957; ARB08605.1; -; mRNA.
DR BRENDA; 4.2.3.57; 4863.
DR BRENDA; 4.2.3.89; 4863.
DR UniPathway; UPA00213; -.
DR GO; GO:0080017; F:alpha-humulene 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:1901937; P:beta-caryophyllene 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 InterPro; IPR019734; TPR_repeat.
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.
DR PROSITE; PS50005; TPR; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..559
FT /note="Terpene synthase 1"
FT /id="PRO_0000454951"
FT MOTIF 312..316
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 559 AA; 64936 MW; 2CCC2217B4782385 CRC64;
MACVSDLVAF TQPLIIGAKP LEIVRRSAAF HPNVWGDYFL KLSQDEKKLE SMRERAKVLK
EKVLKKLSTI EGGERLELID TLYHLGVAYN FEKEIEEALE KIYKAYDEDA TQDNLCTLAL
RFRLLRQHGW NASSDVFNKF KETKNGNFKE SVASDVLGML SLYEASYVGT KEDKILEEAI
SFTTRNLSAA LPNMEPLLAE RVAHSLELPL HKRLQRLEAR YFITMYEKNN AHDEMLLEYA
KLDYNLLQAL HQNEMKELTK WWTKIDLVGK MKFPRDRVTE CYFWPLGAFF EPQHSRGRIF
ATKITQLTSI IDDLYDVYGT QEELQLFTDV IQRWDMNAKK SLPDYIKPLY EALLSTLKDF
EEELSLEGNA YRASFMQQAM KNICMAYFDE AKWYNRGTTP KVEEYLNSAE ISCGYPVVAT
ACFTGAGEIT TKKLLEWIQS QPKYMKDTCR LCRIVDDIKT YKFEEERGHV ASVVACYMEE
HKCNEDEALE KLNEDVMNTW KDINKACMRP TPFPMVVMNI IRNLSRVMEI LYQFGDGYTF
ADTVTKERLN LLLKDPIPV
