TPS4_PHYPO
ID TPS4_PHYPO Reviewed; 337 AA.
AC P9WEY4;
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 4 {ECO:0000303|PubMed:31839833};
DE Short=TPS4 {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=4.2.3.57 {ECO:0000269|PubMed:31839833};
DE AltName: Full=Terpene cyclase TPS4 {ECO:0000305};
GN Name=TPS4 {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 alpha-muurolene, (-)-beta-caryophyllene, and one
CC unidentified sesquiterpene (PubMed:31839833). TPS4 shows only trace
CC monoterpene synthase activity with geranyl diphosphate (GPP) as
CC substrate and produces very small amounts of myrcene (PubMed:31839833).
CC P.polycephalum has a unique biology and these volatile terpenoids could
CC function in internal communication of P.polycephalum, to mark the
CC territory that have been explored, or they may be involved in
CC chemotaxis (Probable). {ECO:0000269|PubMed:31839833,
CC ECO:0000305|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 -!- 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; MN523655; QKE43664.1; -; mRNA.
DR AlphaFoldDB; P9WEY4; -.
DR SMR; P9WEY4; -.
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 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..337
FT /note="Terpene synthase 4"
FT /id="PRO_0000452098"
FT MOTIF 94..98
FT /note="D(D/E)XX(D/E) motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT MOTIF 241..249
FT /note="NSE motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT MOTIF 320..327
FT /note="WxxxxxRY motif"
FT /evidence="ECO:0000305|PubMed:31839833"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 337 AA; 38751 MW; 54EC1DAA32005918 CRC64;
MSCKSNTLAK NYTNHPLRIN EIHLPWKPTI PNTHYEFVRA QVVDLLNELG LCEDKKERDR
RDGVIMLASY MYPEAGPQEL LFGTMYVLWL FFFDDIFDES KFLKEECNQA AERSLHIFRT
GKAPEKNAKL NFSIVQLEDL LLRIFAMAND LAKSSDITAR FMKSCEIYFV DGAVPMENFR
QMKTLPKLEE YLAVRTIDGG AAACIACFEI VAHLDLSDDI VNEPRVLRMC EIAGQQIAYA
NDIYSYHREK LHNNSMNSLN IRCQTLSFED ALTEQIAQLN GWVQEFETLK QSLAESALWE
NSLKMYITGM ENIVMGCKVW SESCTRYNLK SLLTVVV
