TPSLS_PICXS
ID TPSLS_PICXS Reviewed; 578 AA.
AC F2XFA0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Longifolene synthase {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.58 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Lonf {ECO:0000303|PubMed:21385377};
DE Short=PgxeTPS-Lonf {ECO:0000303|PubMed:21385377};
GN Name=TPS-Lonf {ECO:0000303|PubMed:21385377};
OS Picea engelmannii x Picea glauca (Hybrid white spruce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=373101;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. Fa1-1028;
RX PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA Dullat H.K., Bohlmann J.;
RT "Transcriptome mining, functional characterization, and phylogeny of a
RT large terpene synthase gene family in spruce (Picea spp.).";
RL BMC Plant Biol. 11:43-43(2011).
CC -!- FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of
CC sesquiterpene natural products included in conifer oleoresin secretions
CC and volatile emissions; these compounds contribute to biotic and
CC abiotic stress defense against herbivores and pathogens
CC (PubMed:21385377). Catalyzes the conversion of (2E,6E)-farnesyl
CC diphosphate (FPP) to longifolene (PubMed:21385377).
CC {ECO:0000269|PubMed:21385377}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + longifolene;
CC Xref=Rhea:RHEA:25464, ChEBI:CHEBI:6530, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.58;
CC Evidence={ECO:0000269|PubMed:21385377};
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: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:21385377}.
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
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. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ426158; ADZ45515.1; -; mRNA.
DR UniPathway; UPA00924; -.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
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:0016106; P:sesquiterpenoid 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..578
FT /note="Longifolene synthase"
FT /id="PRO_0000454415"
FT MOTIF 331..335
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 578 AA; 67054 MW; 615E336B3FE46998 CRC64;
MAQISKCSSL SAELNESSII SHHHGNLWAD DFIQSLKSSN GAPQYHKRAE KLVEEIKNLV
VSEMKDCNDD LIRRLQMVDI FECLGIDRHF QHEIQVALDY VYRYWNELEG IGIGSRDSLI
KDFNATALGF RALRLHRYNV SSDVLENFKN ENGQFFCSST VEEKEVRCML TLFRASEISF
PGEKVMDEAK AFTTEYLTKV LTGVDVTDVD QSLLREVKYA LEFPWHCSLP RWEARSFIEI
CGQNDSWLKS IMNKRVLELA KLDFNILQCA HHRELQLLSS WWSQSDIAQQ NFYRKRHVEY
YLWVVIGTFE PEFSTCRIAF AKIATLMTIL DDLYDTHGTL EQLKIFTEGV KRWDLSLVDR
LPDYIKITFE FFLNTSNELI AEVAKTQERD MSAYIRKTWE RYLEAYLQEA EWIAARHVPT
FDEYMKNGIS SSGMCILNLY SLLLMGQLLP DDVLEQIHSP SKIHELVELT ARLVDDSKDF
ETKKAGGELA SGIECYVKDN PECTLEDASN HLIGLLDLTV KELNWEFVRH DSVALCFKKF
AFNVARGLRL IYKYRDGFDV SNQEMKTHIF KILIDPLT
