MTPS2_SANAL
ID MTPS2_SANAL Reviewed; 576 AA.
AC F6M8I0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=(+)-alpha-terpineol synthase;
DE EC=4.2.3.112 {ECO:0000269|PubMed:18541135};
DE AltName: Full=(-)-limonene synthase;
DE EC=4.2.3.16 {ECO:0000269|PubMed:18541135};
DE AltName: Full=Beta-bisabolene synthase {ECO:0000303|PubMed:18541135};
DE EC=4.2.3.- {ECO:0000269|PubMed:18541135};
DE AltName: Full=Monoterpene synthase 1 {ECO:0000303|PubMed:21454632};
DE Short=SaMonoTPS1 {ECO:0000303|PubMed:18541135, ECO:0000303|PubMed:21454632};
GN Name=MonoTPS1 {ECO:0000303|PubMed:21454632};
OS Santalum album (White sandalwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Santalales; Santalaceae; Santalum.
OX NCBI_TaxID=35974;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=21454632; DOI=10.1074/jbc.m111.231787;
RA Jones C.G., Moniodis J., Zulak K.G., Scaffidi A., Plummer J.A.,
RA Ghisalberti E.L., Barbour E.L., Bohlmann J.;
RT "Sandalwood fragrance biosynthesis involves sesquiterpene synthases of both
RT the terpene synthase (TPS)-a and TPS-b Subfamilies, including santalene
RT synthases.";
RL J. Biol. Chem. 286:17445-17454(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND COFACTOR.
RX PubMed=18541135; DOI=10.1016/j.abb.2008.05.008;
RA Jones C.G., Keeling C.I., Ghisalberti E.L., Barbour E.L., Plummer J.A.,
RA Bohlmann J.;
RT "Isolation of cDNAs and functional characterisation of two multi-product
RT terpene synthase enzymes from sandalwood, Santalum album L.";
RL Arch. Biochem. Biophys. 477:121-130(2008).
CC -!- FUNCTION: Monoterpene synthase which catalyzes the conversion of (2E)-
CC geranyl diphosphate (GPP) to (R)-alpha-terpineol and (4S)-limonene, as
CC well as small quantities of linalool, myrcene, (-)-alpha-pinene, (+)-
CC sabinene and geraniol (PubMed:18541135). To a lower extent, catalyzes
CC the conversion of (2E,6E)-farnesyl diphosphate (FPP) to beta-bisabolene
CC (PubMed:18541135). {ECO:0000269|PubMed:18541135}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-bisabolene + diphosphate;
CC Xref=Rhea:RHEA:68528, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:18541135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68529;
CC Evidence={ECO:0000269|PubMed:18541135};
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:18541135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32556;
CC Evidence={ECO:0000269|PubMed:18541135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (4S)-limonene + diphosphate;
CC Xref=Rhea:RHEA:12869, ChEBI:CHEBI:15383, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.16;
CC Evidence={ECO:0000269|PubMed:18541135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12870;
CC Evidence={ECO:0000269|PubMed:18541135};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18541135};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18541135};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:18541135}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; JF746815; AEF32532.1; -; Genomic_DNA.
DR AlphaFoldDB; F6M8I0; -.
DR SMR; F6M8I0; -.
DR PRIDE; F6M8I0; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0050552; F:(4S)-limonene synthase activity; 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:0016114; P:terpenoid 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 Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..576
FT /note="(+)-alpha-terpineol synthase"
FT /id="PRO_0000419323"
FT MOTIF 323..327
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 576 AA; 65838 MW; 1104D5D6A68D12BE CRC64;
MDAFATSPTS ALIKAVNCIA HVTPMAGEDS SENRRASNYK PSSWDYEFLQ SLATSHNTAQ
EKHMKMAEKL KEEVKSMIKG QMEPVAKLEL INIVQRLGLK YRFESEIKEE LLSLYKDGTD
AWWVDNLHAT ALRFRLLREN GIFVPQDVFE TFKDKSGKFK SQLCKDVRGL LSLYEASYLG
WEGEDLLDEA KKFSTTNLNN VKESISSNTL GRLVKHALNL PLHWSAARYE ARWFIDEYEK
EENVNPNLLK YAKFDFNIVQ SIHQRELGNL ARWWVETGLD KLSFVRNTLM QNFMWGCAMV
FEPQYGKVRD AAVKQASLIA MVDDVYDVYG SLEELEIFTD IVDRWDITGI DKLPRNISMI
LLTMFNTANQ IGYDLLRDRG FNGIPHIAQA WATLCKKYLK EAKWYHSGYK PTLEEYLENG
LVSISFVLSL VTAYLQTETL ENLTYESAAY VNSVPPLVRY SGLLNRLYND LGTSSAEIAR
GDTLKSIQCY MTQTGATEEA AREHIKGLVH EAWKGMNKCL FEQTPFAEPF VGFNVNTVRG
SQFFYQHGDG YAVTESWTKD LSLSVLIHPI PLNEED
