ATESY_MAGGA
ID ATESY_MAGGA Reviewed; 592 AA.
AC B3TPQ7;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Alpha-terpineol synthase, chloroplastic;
DE Short=Mg17;
DE EC=4.2.3.111;
DE EC=4.2.3.112;
DE Flags: Precursor;
OS Magnolia grandiflora (Southern magnolia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Magnoliaceae;
OC Magnolia.
OX NCBI_TaxID=3406;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18467455; DOI=10.1104/pp.108.115824;
RA Lee S., Chappell J.;
RT "Biochemical and genomic characterization of terpene synthases in Magnolia
RT grandiflora.";
RL Plant Physiol. 147:1017-1033(2008).
CC -!- FUNCTION: Monoterpene synthase converting geranyl diphosphate into
CC alpha-terpineol. In vitro, can also have an sesquiterpene synthase
CC activity, converting farnesyl diphosphate into (E)-alpha-bisabolene
CC (33.1%), alpha-bisabolene (18.7%), beta-sesquiphellandrene (15.8%),
CC beta-bergamotene (12.6%), (Z)-alpha-farnesene (10.4%), and (Z)-alpha-
CC bisabolene (9.4%). {ECO:0000269|PubMed:18467455}.
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:18467455};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (R)-alpha-terpineol +
CC diphosphate; Xref=Rhea:RHEA:32555, ChEBI:CHEBI:300,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057;
CC EC=4.2.3.112; Evidence={ECO:0000269|PubMed:18467455};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:18467455}. Note=The transit peptide can target GFP
CC to both chloroplasts and mitochondria when transiently expressed in a
CC heterologous system.
CC -!- TISSUE SPECIFICITY: Expressed in young developing leaves. Barely
CC detected in tepals, carpels and stamens. {ECO:0000269|PubMed:18467455}.
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}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; EU366430; ACC66282.1; -; Genomic_DNA.
DR AlphaFoldDB; B3TPQ7; -.
DR SMR; B3TPQ7; -.
DR PRIDE; B3TPQ7; -.
DR BioCyc; MetaCyc:MON-14948; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 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 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..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..592
FT /note="Alpha-terpineol synthase, chloroplastic"
FT /id="PRO_0000419801"
FT MOTIF 342..346
FT /note="DDXXD motif"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 592 AA; 67904 MW; C73FB6E07B118729 CRC64;
MALKLLFQCS PCSPSSLAPL QPVLVLVRPP SGAKARRNLR CCASTQVTEL MTARRSANYH
PNIWDYDSVQ SLTSDYKAYT YLERVEKLKE DVRRTLQEAV GLLDQLELVD CIHRLGVGYH
FDKEIKEILK TISTEPNNMG LIDGDLYAMA LYFRLLRQHG YEVPQGVFNR FMDDSSSFKA
SLCNDVKGML SLYEASYLAL EGETTLDEAK AFTYRHLRGL KGNIDSNLKG LVEHALELPL
HWRVLRLEAR WYIDTYERME DMNPLLLELA KLDFNIVQNV YQGQVRKMSG WWKDLGLGQK
LGFARDRLME GFLWTIGVKF EPQFAQCREV LTKINQLITT IDDVYDVYGS LEELELFTKA
VDRWDTNAME ELPEYMKICF LALYNTVNEI AYDTLKEQGV DVIPYLQKSW ADLCKAYLVE
ARWYYSGYTP TLDEYLNNAW ISIAGPVILV HAYVSMIQMI TKEALLDCVG SYESIMQWSS
MILRLADDLA TSTDELERGD VPKSIQCYMH ENTASEVVAR EQMRARISDI WKKMNKDVAL
SPLPQPFKAA AVNLARMAQC MYQHGDGHGN PHRESKDHIL SLVVEPIQLM ES
