SELNS_PICSI
ID SELNS_PICSI Reviewed; 575 AA.
AC Q20HU6; C0PSY9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Delta-selinene-like synthase, chloroplastic {ECO:0000303|PubMed:16415217};
DE Short=PsTPS-Sell {ECO:0000303|PubMed:16415217};
DE EC=4.2.3.76 {ECO:0000250|UniProtKB:O64404};
DE Flags: Precursor;
GN Name=TPS-Sell {ECO:0000303|PubMed:16415217};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY WOUNDING.
RX PubMed=16415217; DOI=10.1104/pp.105.071803;
RA Byun-McKay A., Godard K.-A., Toudefallah M., Martin D.M., Alfaro R.,
RA King J., Bohlmann J., Plant A.L.;
RT "Wound-induced terpene synthase gene expression in Sitka spruce that
RT exhibit resistance or susceptibility to attack by the white pine weevil.";
RL Plant Physiol. 140:1009-1021(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-396.
RC STRAIN=cv. FB3-425; TISSUE=Bark;
RA Reid K.E., Liao N., Ralph S., Kolosova N., Oddy C., Moore R., Mayo M.,
RA Wagner S., King J., Yanchuk A., Holt R., Jones S., Marra M., Ritland C.E.,
RA Ritland K., Bohlmann J.;
RT "Full length sequence-verified cDNA sequences from Sitka spruce (Picea
RT sitchensis).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sesquiterpene synthase (sesqui-TPS) involved in the
CC biosynthesis of sesquiterpene natural products (PubMed:16415217).
CC Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into delta-
CC selinene (By similarity). {ECO:0000250|UniProtKB:O64404,
CC ECO:0000303|PubMed:16415217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-delta-selinene +
CC diphosphate; Xref=Rhea:RHEA:30423, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49279, ChEBI:CHEBI:175763; EC=4.2.3.76;
CC Evidence={ECO:0000250|UniProtKB:O64404};
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:0000303|PubMed:16415217}.
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000303|PubMed:16415217}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Accumulates in apical leaders upon wounding in both
CC resistant and susceptible to white pine weevil (Pissodes strobi)
CC plants. {ECO:0000269|PubMed:16415217}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ195276; ABA86249.1; -; mRNA.
DR EMBL; BT071470; ACN40929.1; -; mRNA.
DR BioCyc; MetaCyc:MON-14954; -.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0009611; P:response to wounding; IEP: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 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..575
FT /note="Delta-selinene-like synthase, chloroplastic"
FT /id="PRO_0000455263"
FT MOTIF 325..329
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 325
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 85
FT /note="Q -> E (in Ref. 2; ACN40929)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="G -> A (in Ref. 2; ACN40929)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> V (in Ref. 2; ACN40929)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="Q -> L (in Ref. 2; ACN40929)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="K -> E (in Ref. 2; ACN40929)"
FT /evidence="ECO:0000305"
FT CONFLICT 390..396
FT /note="KANWQRY -> NELAAIC (in Ref. 2; ACN40929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 66615 MW; 552D477373A1C0E9 CRC64;
MAQISESAAI PRRTANHHGN VWDDDLILSL DSPYGAPAYY ERVANLIEEM KHLLLREMED
SNHDLIRRLQ IVDTLECLGI DRHFQHEIKT AALDYVYRCW NEKGIGMGSS DSGSKDLDAT
ALGLRALRLH RYNVSSGVLE NFKDENGKFF CNLTGDKRVR SMLSLLRASE ISFPGEKVMQ
EAKAFTREYL TQVLAGRGDV TDVDQSLLRE VKYALEFPWH WSVPRWEARS FIEIYGQNHS
WLKSNINQKV LELAKLDFNI LQCIHQKEIQ FIVRWWRESE IAQLNFYRKR HVEFYFWVVI
CIFEPEFSQS RIAFAKICTV ATVLDDLYDT HGMLDELKTV TEGVSRWDLP LIDDLPDNIK
IAFQFFFNTA NELAVEVVKK QGRDMIALLK ANWQRYVESY LQEAEWIATR HVPSFDEYIK
NARASSGMCI GNLIPLLLLG QLLANNIVEQ IHSPSKIQEL SELTIRLIDD IRDFEDEKER
GEIASAIECY MKDNPDSTVE NALNHLEGIL HLSLEELNWE FIKQDTVPLC CKKFTFNIVR
GLQFVYKYGD GLSISNKEVK DQIFKILIDQ VPIEE
