TPS1_PHYPO
ID TPS1_PHYPO Reviewed; 334 AA.
AC P9WEY7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Terpene synthase 1 {ECO:0000303|PubMed:31839833};
DE Short=TPS1 {ECO:0000303|PubMed:31839833};
DE EC=4.2.3.- {ECO:0000269|PubMed:31839833};
DE EC=4.2.3.125 {ECO:0000269|PubMed:31839833};
DE EC=4.2.3.126 {ECO:0000269|PubMed:31839833};
DE EC=4.2.3.15 {ECO:0000269|PubMed:31839833};
DE EC=4.2.3.57 {ECO:0000269|PubMed:31839833};
DE AltName: Full=Terpene cyclase TPS1 {ECO:0000305};
GN Name=TPS1 {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, FUNCTION, AND CATALYTIC ACTIVITY.
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 catalyzes the cyclization of farnesyl
CC diphosphate (FPP) into a mixture of sesquiterpenes with gamma-muurolene
CC as the most abundant compound and (-)-beta-caryophyllene, alpha-
CC muurolene, and 4 unidentified sesquiterpenes as minor compoundss
CC (PubMed:31839833). TPS1 shows also monoterpene synthase activity and
CC can also use geranyl diphosphate (GPP) as a substrate to convert it
CC into a mixture of cyclic and acyclic monoterpenes, including myrcene
CC and linalool (PubMed:31839833). P.polycephalum has a unique biology and
CC these 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 -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene;
CC Xref=Rhea:RHEA:33107, ChEBI:CHEBI:33019, ChEBI:CHEBI:64798,
CC ChEBI:CHEBI:175763; EC=4.2.3.126;
CC Evidence={ECO:0000269|PubMed:31839833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33108;
CC Evidence={ECO:0000269|PubMed:31839833};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate;
CC Xref=Rhea:RHEA:33103, ChEBI:CHEBI:33019, ChEBI:CHEBI:64797,
CC ChEBI:CHEBI:175763; EC=4.2.3.125;
CC Evidence={ECO:0000269|PubMed:31839833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33104;
CC Evidence={ECO:0000269|PubMed:31839833};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:31839833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:31839833};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:31839833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|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; MN523652; QKE43661.1; -; mRNA.
DR AlphaFoldDB; P9WEY7; -.
DR SMR; P9WEY7; -.
DR GO; GO:0080016; F:(-)-E-beta-caryophyllene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..334
FT /note="Terpene synthase 1"
FT /id="PRO_0000452097"
FT MOTIF 82..86
FT /note="D(D/E)XX(D/E) motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT MOTIF 230..238
FT /note="NSE motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT MOTIF 309..316
FT /note="WxxxxxRY motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 334 AA; 38880 MW; 6356556FF9CE8507 CRC64;
MNHPLRIHEI RLPWKHTPMN PHYAFVREQI VALLNELGLC EEEKEKDRRD GVITMGAYIY
PDAGPNELLF GTLFVLWLFF FDDIFDESKF LKGESSQAAE RTLQMFRTRQ PPVNATTGLS
MGIVQLEKLL LRIFKMAKDL AHGPYVISRF METCEFYITE GAIPMDKFRF RKELPKLDEY
LAVRTIDGAG EACIVCSEIV AHLALPEHII NEPRIKRMRE ITGQQIVYSN DIYSYHREKI
HNNSVNALNI RCLTKSFNDA LTDQINQVNE WVLEFEALKN SLYESTLWEN NLDVYITGME
NTMMGCKIWS ESCTRYDLNA LLHITPDKNE FPER
