ID   TPS3_PHYPO              Reviewed;         353 AA.
AC   P9WEY5;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Terpene synthase 3 {ECO:0000303|PubMed:31839833};
DE            Short=TPS3 {ECO:0000303|PubMed:31839833};
DE            EC=4.2.3.- {ECO:0000305|PubMed:31839833};
DE   AltName: Full=Terpene cyclase TPS3 {ECO:0000305};
GN   Name=TPS3 {ECO:0000303|PubMed:31839833};
OS   Physarum polycephalum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC   Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX   NCBI_TaxID=5791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, AND FUNCTION.
RX   PubMed=31839833; DOI=10.3762/bjoc.15.281;
RA   Chen X., Koellner T.G., Xiong W., Wei G., Chen F.;
RT   "Emission and biosynthesis of volatile terpenoids from the plasmodial slime
RT   mold Physarum polycephalum.";
RL   Beilstein J. Org. Chem. 15:2872-2880(2019).
CC   -!- FUNCTION: Terpene synthase that may be involved in the production of
CC       volatile terpenoids (PubMed:31839833). Does not show detectable terpene
CC       products with either farnesyl diphosphate (FPP) or geranyl diphosphate
CC       (GPP) (PubMed:31839833). P.polycephalum has a unique biology and these
CC       volatile terpenoids could function in internal communication of
CC       P.polycephalum, to mark the territory that have been explored, or they
CC       may be involved in chemotaxis (Probable). {ECO:0000269|PubMed:31839833,
CC       ECO:0000305|PubMed:31839833}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9UR08};
CC   -!- DOMAIN: The 2 conserved active-site motifs D(D/E)XX(D/E) and NSE are
CC       required for coordinating the divalent metal ions that stabilize the
CC       PPi moiety of the substrate. {ECO:0000250|UniProtKB:Q9UR08}.
CC   -!- DOMAIN: The C-terminal WxxxxxRY motif is frequently found in terpene
CC       synthases and is important to guide product formation.
CC       {ECO:0000305|PubMed:31839833}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; MN523654; QKE43663.1; -; mRNA.
DR   AlphaFoldDB; P9WEY5; -.
DR   SMR; P9WEY5; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..353
FT                   /note="Terpene synthase 3"
FT                   /id="PRO_0000452100"
FT   MOTIF           118..122
FT                   /note="D(D/E)XX(D/E) motif"
FT                   /evidence="ECO:0000305|PubMed:31839833"
FT   MOTIF           261..269
FT                   /note="NSE motif"
FT                   /evidence="ECO:0000305|PubMed:31839833"
FT   MOTIF           342..349
FT                   /note="WxxxxxRY motif"
FT                   /evidence="ECO:0000305|PubMed:31839833"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   SITE            115
FT                   /note="Plays a critical role in the stabilization of
FT                   intermediate cation"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   353 AA;  40041 MW;  375EA8D6EF9F890B CRC64;
     MEVLRQMLVH KANNSSMSTH KGLNRTEPVR MTYDHCELLG QLSTLNFSAA SNTFSSGYNT
     TIKGSAPKTI QTVSSLFSKD ITKAMSDIGN LVARMFPTAS AERAAVILDI TVFGFIADDL
     LEDAALSSDS EAFDKLHMLM LRLVRNDSFS EDEYPEYQNL IRFTRPIFTK FQALASRTLL
     NRFAYTYQEY LQGVQWEASL QPNQIPDFET CKNVKRHVGA WLCYFVLAEF AREIEVPITV
     RGNLEVQKFV TLACDIASYD NDTFLLKKEI RDGVVSNTIV ITYLHGAKRL QDALDRILEM
     RKQTESEILA ITSNLPHFGK DDKVAREYIN ALTCVIGGNF EWCSKTTRYQ DPK