PT30_PINTA
ID PT30_PINTA Reviewed; 628 AA.
AC Q84KL3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=(+)-alpha-pinene synthase, chloroplastic;
DE EC=4.2.3.121;
DE AltName: Full=(+)-(3R:5R)-alpha-pinene synthase;
DE AltName: Full=Synthase II;
DE Flags: Precursor;
GN Name=PT30;
OS Pinus taeda (Loblolly pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3352;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND 3D-STRUCTURE MODELING.
RX PubMed=12623076; DOI=10.1016/s0003-9861(02)00746-4;
RA Phillips M.A., Wildung M.R., Williams D.C., Hyatt D.C., Croteau R.;
RT "cDNA isolation, functional expression, and characterization of (+)-alpha-
RT pinene synthase and (-)-alpha-pinene synthase from loblolly pine (Pinus
RT taeda): stereocontrol in pinene biosynthesis.";
RL Arch. Biochem. Biophys. 411:267-276(2003).
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. Produces mainly (+)-alpha-pinene (97%) with
CC a small amount of (-)-alpha-pinene (3%). {ECO:0000269|PubMed:12623076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1R,5R)-alpha-pinene + diphosphate;
CC Xref=Rhea:RHEA:32575, ChEBI:CHEBI:28261, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.121;
CC Evidence={ECO:0000269|PubMed:12623076};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:12623076};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:12623076};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000305|PubMed:12623076};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:12623076};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47 uM for geranyl diphosphate {ECO:0000269|PubMed:12623076};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:12623076};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; AF543530; AAO61228.1; -; mRNA.
DR AlphaFoldDB; Q84KL3; -.
DR SMR; Q84KL3; -.
DR PRIDE; Q84KL3; -.
DR KEGG; ag:AAO61228; -.
DR BRENDA; 4.2.3.121; 4861.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0050550; F:pinene synthase activity; IDA:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; 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:0033383; P:geranyl diphosphate metabolic 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 Potassium; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..628
FT /note="(+)-alpha-pinene synthase, chloroplastic"
FT /id="PRO_0000419231"
FT MOTIF 379..383
FT /note="DDXXD motif"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
SQ SEQUENCE 628 AA; 71496 MW; 4208222612256837 CRC64;
MALVSAVPLN SKLCLRRTLF GFSHELKAIH STVPNLGMCR GGKSIAPSMS MSSTTSVSNE
DGVPRRIAGH HSNLWDDDSI ASLSTSYEAP SYRKRADKLI GEVKNIFDLM SVEDGVFTSP
LSDLHHRLWM VDSVERLGID RHFKDEINSA LDHVYSYWTE KGIGRGRESG VTDLNSTALG
LRTLRLHGYT VSSHVLDHFK NEKGQFTCSA IQTEGEIRDV LNLFRASLIA FPGEKIMEAA
EIFSTMYLKD ALQKIPPSGL SQEIEYLLEF GWHTNLPRME TRMYIDVFGE DTTFETPYLI
REKLLELAKL EFNIFHSLVK RELQSLSRWW KDYGFPEITF SRHRHVEYYT LAACIANDPK
HSAFRLGFGK ISHMITILDD IYDTFGTMEE LKLLTAAFKR WDPSSIECLP DYMKGVYMAV
YDNINEMARE AQKIQGWDTV SYARKSWEAF IGAYIQEAKW ISSGYLPTFD EYLENGKVSF
GSRITTLEPM LTLGFPLPPR ILQEIDFPSK FNDLICAILR LKGDTQCYKA DRARGEEASA
VSCYMKDHPG ITEEDAVNQV NAMVDNLTKE LNWELLRPDS GVPISYKKVA FDICRVFHYG
YKYRDGFSVA SIEIKNLVTR TVVETVPL
