ID   MTPS1_SANAL             Reviewed;         576 AA.
AC   B5A434;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=(+)-alpha-terpineol synthase;
DE            Short=SaMonoTPS1;
DE            EC=4.2.3.112;
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 [MRNA], FUNCTION, COFACTOR, AND CATALYTIC ACTIVITY.
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 producing mainly (+)-alpha-terpineol
CC       (44%) and (-)-limonene (33.6%) and lower amounts of (E)-geraniol
CC       (5.9%), linalool (5.0%), myrcene (3.4%), (-)-alpha-pinene (3.3%), (+)-
CC       sabinene (3.0%) and alpha-terpinolene (1.6%).
CC       {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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:18541135};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000305|PubMed:18541135};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC       {ECO:0000305|PubMed:18541135};
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU798692; ACF24767.1; -; mRNA.
DR   AlphaFoldDB; B5A434; -.
DR   SMR; B5A434; -.
DR   KEGG; ag:ACF24767; -.
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   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_0000419322"
FT   MOTIF           323..327
FT                   /note="DDXXD motif"
FT   BINDING         323
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         477
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   576 AA;  65844 MW;  8F6E82805C6DFF99 CRC64;
     MDAFATSPTS ALIKAVNCIA HVTPMAGEDS SENRRASNYK PSTWDYEFLQ SLATSHNTVQ
     EKHMKMAEKL KEEVKSMIKG QMEPVAKLEL INILQRLGLK YRFESEIKEE LFSLYKDGTD
     AWWVDNLHAT ALRFRLLREN GIFVPQDVFE TLKDKSGKFK SQLCKDVRGL LSLYEASYLG
     WEGEDLLDEA KKFSTTNLNN VKESISSNTL GRLVKHALNL PLHWSAARYE ARWFIDEYEK
     EENVNPNLLK YAKLDFNIVQ SIHQQELGNL ARWWVETGLD KLSFVRNTLM QNFMWGCAMV
     FEPQYGKVRD AAVKQASLIA MVDDVYDVYG SLEELEIFTD IVDRWDITGI DKLPRNISMI
     LLTMFNTANQ IGYDLLRDRG FNGIPHIAQA WATLCKKYLK EAKWYHSGYK PTLEEYLENG
     LVSISFVLSL VTAYLQTEIL ENLTYESAAY VNSVPPLVRY SGLLNRLYND LGTSSAEIAR
     GDTLKSIQCY MTQTGATEEA AREHIKGLVH EAWKGMNKCL FEQTPFAEPF VGFNVNTVRG
     SQFFYQHGDG YAVTESWTKD LSLSVLIHPI PLNEED