PT10_PINTA
ID PT10_PINTA Reviewed; 627 AA.
AC Q84KL4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=(-)-alpha-terpineol synthase, chloroplastic;
DE EC=4.2.3.111;
DE Flags: Precursor;
GN Name=PT10;
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, AND CATALYTIC ACTIVITY.
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 57.3% alpha-terpineol (15.1%
CC (+)/84.9% (-)), 27.6% limonene (25.2% (+)/74.8% (-)), 8% terpinolene,
CC 4.7% beta-pinene (14.8% (+)/85.2% (-)), 1.3% alpha-pinene (100% (+))
CC and 1.1% myrcene. {ECO:0000269|PubMed:12623076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (S)-alpha-terpineol +
CC diphosphate; Xref=Rhea:RHEA:32551, ChEBI:CHEBI:128,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC EC=4.2.3.111; Evidence={ECO:0000269|PubMed:12623076};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
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; AF543529; AAO61227.1; -; mRNA.
DR AlphaFoldDB; Q84KL4; -.
DR SMR; Q84KL4; -.
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:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0033383; P:geranyl diphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0043693; P:monoterpene 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..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..627
FT /note="(-)-alpha-terpineol synthase, chloroplastic"
FT /id="PRO_0000419233"
FT MOTIF 378..382
FT /note="DDXXD motif"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 627 AA; 71884 MW; FACA215FA7739B63 CRC64;
MDLISVLPSA SKSCVCLHKP LSSSTHKLKP FCKTIRILVM PRRWEFARPS MSLSTVASED
DIQRRTGGYL SNLWNDDVIQ FLSTPYGELA YRERAERLID EVRDIFSSMS LEDGEFSDLI
QRLWMVDNVE RLGIDRHFKN EIKSALDYVY SYWSEKGIGC GTKSIITNLN STALGFRTLR
LHGYPVSADV LKHFRNQIGQ FVSCPSETEE DIRIMVNLYR ASLIAFPVAF PGEKVMEEAE
SFSEKYLKET LQKIPDCSLS REIGDVLEHG WHTNLPRLEA RNYIDVFGQD TKNMEPNRKT
EKLLELAKLE FNIFQSIQKT ELESLLRWWN DSGSPQITFT RHRHVEYYTL ASCIAFEPQH
SGFRLGFAKA CHILTVLDDM YDLFGTVDEL KLFTAAIKRW DPSATDCLPQ YMKGIYMMVY
NTVNEMSAEA QKAQGRDTLN YARQAWEDCL DSHMQEAKWI ATGFLPTFEE YLENGKVSSA
HRVSALQPML TMDIPFPPHI LKEVDFPSNL NDLACAMLRL RGDTRCYQAD RARGEETSCI
SCYMKDNPGA TEEDALNHLN VMISGVIKEL NWELLKPNSS VPISSKKINF DITRAFHYGY
KYRDGYSVSS VETKSLVMRT LLEPVPL
