PINS1_PICGL
ID PINS1_PICGL Reviewed; 627 AA.
AC F2XF95;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=(-)-alpha-pinene synthase 1, chloroplastic {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.119 {ECO:0000269|PubMed:21385377};
DE AltName: Full=(-)-beta-pinene synthase 1 {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.120 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Pin-1 {ECO:0000303|PubMed:21385377};
DE Short=PgTPS-Pin-1;
DE Flags: Precursor;
GN Name=TPS-Pin-1 {ECO:0000303|PubMed:21385377};
OS Picea glauca (White spruce) (Pinus glauca).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3330;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. PG29;
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 monoterpene 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)-geranyl diphosphate
CC (GPP) to (1S,5S)-beta-pinene (PubMed:21385377).
CC {ECO:0000269|PubMed:21385377}.
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:21385377};
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: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: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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; HQ426153; ADZ45507.1; -; mRNA.
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; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..627
FT /note="(-)-alpha-pinene synthase 1, chloroplastic"
FT /id="PRO_0000454408"
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"
SQ SEQUENCE 627 AA; 71378 MW; 74D0B2DF5703AE77 CRC64;
MALVSIAPLA SKSCLHKSLS SSAHELKTIC RTIPTLGMSR RGKSATPSMS MSLTTTVSDD
GVQRRMGDFH SNLWNDDFIQ SLSTSYGEPS YREQAERLIG EVKKMFNSMS SEDGELINPH
NDLIQRVWMV DSVERLGIER HFKNEIKSAL DYVYSYWSEK GIGCGRESVV ADLNSTALGL
RTLRLHGYAV SADVLNLFKD QNGQFACSPS QTEEEIRSVL SLYRASLIAF PGEKVMEEAE
IFSAKYLEEA LQKISVSSLS QEIRDVLEYG WHTYLPRMEA RNHIDVFGQD TQNSKSCINT
EKLLELAKLE FNIFHSLQKR ELEYLVRWWK DSGSPQMTFG RHRHVEYYTL ASCIAFEPQH
SGFRLGFAKT CHIITILDDM YDTFGTVDEL ELFTAAMKRW NPSAADCLPE YMKGMYMIVY
DTVNEICQEA EKAQGRNTLD YARQAWDEYL DSYMQEAKWI VTGYLPTFAE YYENGKVSSG
HRTAALQPIL TMDIPFPPHI LKEVDFPSKL NDLACAILRL RGDTRCYKAD RARGEEASSI
SCYMKDNPGV TEEDALDHIN AMISDVIRGL NWELLNPNSS VPISSKKHVF DISRAFHYEY
KYRDGYSVAN IETKSLVKRT VIDPVTL
