TPS31_SOLLC
ID TPS31_SOLLC Reviewed; 555 AA.
AC G5CV46;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Sesquiterpene synthase 31 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE Short=SlTPS31 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE AltName: Full=Viridiflorene synthase TPS31 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.88 {ECO:0000269|PubMed:21818683};
GN Name=TPS31 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION BY JASMONATE, PATHWAY, AND GENE FAMILY.
RC STRAIN=cv. Moneymaker;
RX PubMed=21818683; DOI=10.1007/s11103-011-9813-x;
RA Bleeker P.M., Spyropoulou E.A., Diergaarde P.J., Volpin H., De Both M.T.J.,
RA Zerbe P., Bohlmann J., Falara V., Matsuba Y., Pichersky E., Haring M.A.,
RA Schuurink R.C.;
RT "RNA-seq discovery, functional characterization, and comparison of
RT sesquiterpene synthases from Solanum lycopersicum and Solanum habrochaites
RT trichomes.";
RL Plant Mol. Biol. 77:323-336(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION BY
RP JASMONATE, AND GENE FAMILY.
RC STRAIN=cv. M82;
RX PubMed=21813655; DOI=10.1104/pp.111.179648;
RA Falara V., Akhtar T.A., Nguyen T.T.H., Spyropoulou E.A., Bleeker P.M.,
RA Schauvinhold I., Matsuba Y., Bonini M.E., Schilmiller A.L., Last R.L.,
RA Schuurink R.C., Pichersky E.;
RT "The tomato terpene synthase gene family.";
RL Plant Physiol. 157:770-789(2011).
CC -!- FUNCTION: Sesquiterpene synthase involved in the production of
CC viridiflorene from (E,E)-farnesyl diphosphate (FPP) (PubMed:21818683).
CC Has no activity with (Z,Z)-FPP (PubMed:21818683). Can act with a low
CC efficiency as a monoterpene synthase with geranyl diphosphate as
CC substrate (PubMed:21818683). {ECO:0000269|PubMed:21818683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene;
CC Xref=Rhea:RHEA:31811, ChEBI:CHEBI:33019, ChEBI:CHEBI:63444,
CC ChEBI:CHEBI:175763; EC=4.2.3.88;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31812;
CC Evidence={ECO:0000269|PubMed:21818683};
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:21818683}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stem and leaf trichomes. Detected in
CC roots, fruits and flowers. {ECO:0000269|PubMed:21813655,
CC ECO:0000269|PubMed:21818683}.
CC -!- INDUCTION: Up-regulated by jasmonic acid treatment.
CC {ECO:0000269|PubMed:21813655, ECO:0000269|PubMed:21818683}.
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:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; JN402396; AEM23833.1; -; mRNA.
DR EMBL; JN412082; AEP82774.1; -; Genomic_DNA.
DR RefSeq; NP_001239040.1; NM_001252111.1.
DR AlphaFoldDB; G5CV46; -.
DR SMR; G5CV46; -.
DR STRING; 4081.Solyc01g101170.2.1; -.
DR PaxDb; G5CV46; -.
DR PRIDE; G5CV46; -.
DR GeneID; 100820700; -.
DR KEGG; sly:100820700; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR HOGENOM; CLU_003125_7_2_1; -.
DR InParanoid; G5CV46; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; G5CV46; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; G5CV46; differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0016114; P:terpenoid 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 Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..555
FT /note="Sesquiterpene synthase 31"
FT /id="PRO_0000418827"
FT MOTIF 308..312
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
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 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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"
SQ SEQUENCE 555 AA; 64299 MW; BF7E4CD3F76338E5 CRC64;
MAPAAALMSK CQEEEEIVRP VADFSPSLWG DRFHSFSLDN QVAEKYVEEI ETLKEQTRSM
LMSGKTLAEK LNLIDIVERL GIAYHFEKQI DDMLNHIFNI DPNFEAHEYN DLCTLSLQFR
ILRQHGYYIS PKIFSRFQDA NGKFKESLCD DIRGILNLYE ASHVRTHGED TLEEALAFST
AHLESAAPHL KSPLSKQVTH ALEQSLHKSI PRVETRYFIS IYEEEELKND VFLRFAKLDF
NLLQMLHKQE LSEVSRWWKD LDFVTTLPYA RDRAVECYFW TMGVYAEPQY SQARVMLAKT
IAMISIVDDT FDAYGIVKEL EVYTDAIQRW DVSQIDRLPE YMKISYKALL DLYNDYETEL
SNDGRSDVVQ YAKERMKEIV RNYFVEAKWF IEGYMPPVSE YLSNALATST YYLLTTTSYL
GMKSATKKDF EWLAKNPKIL EANVTLCRVI DDIATYEVEK GRGQIATGIE CYMRDYGVST
QVAMDKFQEM AETAWKDVNE GILRPTPVSA KILTRILNLA RIIDVTYKHN QDGYTHPEKV
LKPHIIALLV DSIEI
