PINS2_PICSI
ID PINS2_PICSI Reviewed; 627 AA.
AC Q6XDB5; C0PT91;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=(-)-alpha-pinene synthase 2, chloroplastic {ECO:0000303|PubMed:12970502};
DE EC=4.2.3.119 {ECO:0000269|PubMed:12970502};
DE AltName: Full=(-)-(1S,5S)-pinene synthase {ECO:0000303|PubMed:12970502};
DE AltName: Full=(-)-beta-pinene synthase 2 {ECO:0000303|PubMed:12970502};
DE EC=4.2.3.120 {ECO:0000269|PubMed:12970502};
DE AltName: Full=Beta-geraniolene synthase;
DE AltName: Full=Pinene synthase, chloroplastic {ECO:0000303|PubMed:12970502};
DE Short=PsTPS2;
DE Flags: Precursor;
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], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY
RP WOUNDING AND INSECT ATTACK, AND PATHWAY.
RX PubMed=12970502; DOI=10.1104/pp.103.022723;
RA McKay S.A., Hunter W.L., Godard K.A., Wang S.X., Martin D.M., Bohlmann J.,
RA Plant A.L.;
RT "Insect attack and wounding induce traumatic resin duct development and
RT gene expression of (-)-pinene synthase in Sitka spruce.";
RL Plant Physiol. 133:368-378(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC 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.
RN [3]
RP MUTAGENESIS OF SER-538.
RX PubMed=19181671; DOI=10.1074/jbc.m807140200;
RA Green S., Squire C.J., Nieuwenhuizen N.J., Baker E.N., Laing W.;
RT "Defining the potassium binding region in an apple terpene synthase.";
RL J. Biol. Chem. 284:8661-8669(2009).
CC -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC response to insect attack or other injury. Involved in monoterpene
CC (C10) olefins biosynthesis. A mixture of alpha- and beta-pinene (35:10)
CC is produced by this enzyme. {ECO:0000269|PubMed:12970502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,5S)-alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:25488, ChEBI:CHEBI:28660, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.119;
CC Evidence={ECO:0000269|PubMed:12970502};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1S,5S)-beta-pinene + diphosphate;
CC Xref=Rhea:RHEA:25496, ChEBI:CHEBI:28359, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.120;
CC Evidence={ECO:0000269|PubMed:12970502};
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: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:12970502}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: By wounding and insect attack.
CC {ECO:0000269|PubMed:12970502}.
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; AY237645; AAP72020.1; -; mRNA.
DR EMBL; BT071578; ACN41031.1; -; mRNA.
DR AlphaFoldDB; Q6XDB5; -.
DR SMR; Q6XDB5; -.
DR KEGG; ag:AAP72020; -.
DR BRENDA; 4.2.3.119; 8974.
DR BRENDA; 4.2.3.120; 8974.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0046248; P:alpha-pinene 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:0016099; P:monoterpenoid 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 Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..627
FT /note="(-)-alpha-pinene synthase 2, chloroplastic"
FT /id="PRO_0000401484"
FT MOTIF 378..382
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT MUTAGEN 538
FT /note="S->A: 30% decrease in monoterpene synthase
FT activity."
FT /evidence="ECO:0000269|PubMed:19181671"
FT MUTAGEN 538
FT /note="S->K: 8-fold higher monoterpene synthase activity in
FT absence of potassium, and loss of dependence on potassium."
FT /evidence="ECO:0000269|PubMed:19181671"
FT CONFLICT 6..12
FT /note="VAPMASR -> IAPLASK (in Ref. 2; ACN41031)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="T -> M (in Ref. 2; ACN41031)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="R -> K (in Ref. 2; ACN41031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 71384 MW; 9BCB2C98916F1195 CRC64;
MALVSVAPMA SRSCLHKSLS SSAHELKTIC RTIPTLGMSR RGKSATPSMS MSLTTTVSDD
GVQRRMGDFH SNLWNDDFIQ SLSTSYGEPS YRERAERLIG EVKKMFNSMS SEDGELISPH
NDLIQRVWMV DSVERLGIER HFKNEIKSAL DYVYSYWSEK GIGCGRESVV ADLNSTALGF
RTLRLHGYAV SADVLNLFKD QNGQFACSPS QTEEEIRSVL NLYRASLIAF PGEKVMEEAE
IFSAKYLEES LQKISVSSLS QEIRDVLEYG WHTYLPRMEA RNHIDVFGQD TQNSKSCINT
EKLLELAKLE FNIFHSLQKR ELEYLVRWWK DSGSPQMTFC RHRHVEYYTL ASCIAFEPQH
SGFRLGFAKA CHIITILDDM YDTFGTVDEL ELFTAAMKRW DPSAADCLPE YMKGVYLILY
DTVNETSREA EKAQGRDTLD YARRAWDDYL DSYMQEAKWI ATGYLPTFAE YYENGKVSSG
HRTSALQPIL TMDIPFPPHI LKEVDFPSKL NDLASAILRL RGDTRCYKAD RARGEEASSI
SCYMKDNPGA TEEDALDHIN AMISDVIRGL NWELLNPNSS VPISSKKHVF DISRAFHYGY
KYRDGYSVAN IETKSLVRRT VIDPVTL
