TPS2_PHYPO
ID TPS2_PHYPO Reviewed; 347 AA.
AC P9WEY6;
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 2 {ECO:0000303|PubMed:31839833};
DE Short=TPS2 {ECO:0000303|PubMed:31839833};
DE EC=4.2.3.- {ECO:0000305|PubMed:31839833};
DE AltName: Full=Terpene cyclase TPS2 {ECO:0000305};
GN Name=TPS2 {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; MN523653; QKE43662.1; -; mRNA.
DR AlphaFoldDB; P9WEY6; -.
DR SMR; P9WEY6; -.
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..347
FT /note="Terpene synthase 2"
FT /id="PRO_0000452099"
FT MOTIF 103..107
FT /note="D(D/E)XX(D/E) motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT MOTIF 247..255
FT /note="NSE motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT MOTIF 329..336
FT /note="WxxxxxRY motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 100
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 347 AA; 39958 MW; 6339F839DEC57C2C CRC64;
MKKKTVLYKY PMMAQMSYDQ QELLDQLPHL DFSHFHSAFK SGFNASINAM EEKALRNAAL
YFPAEDVKML GDMGGLVARM FYKASDERGA VLLDIFVFAF ITDDLLEKPE LRRHNENYRK
LQILILKLVR NESFPEKDYP EWRNLITFSR PIFSKFQNLA SPTLFHRFAF QYQEYLQGVD
WEASIRSPNP VPDIETCKHV KRHLSGGQVA FVLAEFSREI EVPIAVRAHP GMQKFCSLAS
DLASYDNDIF SLKKEVRDGV VCNTILFLYL HGITKSLQAA VDRVVHMRKQ TEREIISLIN
DLPQFGRDNA VAQEYISAIT RCIGGNFEWC SKSTRYHVAS SLPHSKL
