PT1_PINTA
ID PT1_PINTA Reviewed; 629 AA.
AC Q84KL6;
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=4.2.3.119;
DE AltName: Full=(+)-(3S:5S)-alpha-pinene synthase;
DE AltName: Full=Synthase I;
DE Flags: Precursor;
GN Name=PT1;
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 (79%) and
CC lesser amounts of (-)-beta-pinene (4.2%), nearly racemic mixtures of
CC camphene (2.8% (+)/2.2% (-)) and limonene (2.4% (+)/3.7% (-)), as well
CC as small amounts of (+)-alpha-pinene (3.3%) and (+)-beta-pinene (2.4%).
CC {ECO:0000269|PubMed:12623076}.
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: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=1.4 uM for geranyl-diphosphate {ECO:0000269|PubMed:12623076};
CC pH dependence:
CC Optimum pH is 7.0. {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; AF543527; AAO61225.1; -; mRNA.
DR AlphaFoldDB; Q84KL6; -.
DR SMR; Q84KL6; -.
DR KEGG; ag:AAO61225; -.
DR BRENDA; 4.2.3.119; 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..629
FT /note="(-)-alpha-pinene synthase, chloroplastic"
FT /id="PRO_0000419232"
FT MOTIF 380..384
FT /note="DDXXD motif"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
SQ SEQUENCE 629 AA; 71807 MW; 39DDCD936BCB1791 CRC64;
MSPVSVISLP SDLCLPTSFI DRSGRELIPL HITIPNVAMR RQGKLMTRAS MSMNLRTAVS
DDAVIRRRGD FHSNLWDDDL IQSLSSPYGE PSYRERAERL IGEVKNSFNS MSNEDGESIT
PLDDLIQRLW MVDSVERLGI DRHFKKEIKS ALDHVYRYWS EKGIGCGRES VVTDLNSTAL
GLRTLRLHGY DVSADVLNHF KNQSGQFACT LKQTEDQIRT VLNLYRASLI AFPGEKVMDE
AESFSAKYLK EALQKIPVSS FSREIGDVLE YGWHTYLPRL EARNYIDVFG QDTENSKSYM
KTEKLLELAK LEFNIFHALQ KRELEYLVRW WKGSGSPQMT FCRHRHVEYY TLASCIAFEP
QHSGFRLGFA KACHIITVLD DMYDTFGTLD ELELFTSAIK RWDPSATECL PEYMKGVYMI
VYNTVNEMSQ EADKAQGRDT LNYCRQAWEE YIDAYMQEAK WIASGEVPTF EEYYENGKVS
SGHRVSALQP ILTTDIPFPE HVLKEVDIPS QLNDLASAIL RLRGDTRCYQ ADRARGEEAS
CISCYMKDNP GTTEEDALNH LNAMISDVIK GLNWELLKPN SSVPISAKKH AFDISRAFHC
GYKYRDGYSV ANIETKSLVK RTVIDPVTL
