ID   STS9_POSPM              Reviewed;         344 AA.
AC   A0A348B785;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Sesquiterpene synthase 9 {ECO:0000303|PubMed:30105900};
DE            EC=4.2.3.- {ECO:0000269|PubMed:30105900};
DE   AltName: Full=Terpene cyclase 9 {ECO:0000303|PubMed:30105900};
GN   Name=STS-09 {ECO:0000303|PubMed:30105900};
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Dacryobolaceae; Postia.
OX   NCBI_TaxID=561896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 44394 / Madison 698-R;
RX   PubMed=30105900; DOI=10.1111/1751-7915.13304;
RA   Ichinose H., Kitaoka T.;
RT   "Insight into metabolic diversity of the brown-rot basidiomycete Postia
RT   placenta responsible for sesquiterpene biosynthesis: semi-comprehensive
RT   screening of cytochrome P450 monooxygenase involved in protoilludene
RT   metabolism.";
RL   Microb. Biotechnol. 11:952-965(2018).
CC   -!- FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl
CC       diphosphate (FPP) to a single major sesquiterpene scaffold whose
CC       chemical structure is still unknown. {ECO:0000269|PubMed:30105900}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:I3ZNU9};
CC   -!- DOMAIN: The conserved DDXXD and NSE/DTE motifs are important for the
CC       catalytic activity, presumably through binding to Mg(2+).
CC       {ECO:0000305|PubMed:30105900}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; LC378431; BBD74523.1; -; mRNA.
DR   AlphaFoldDB; A0A348B785; -.
DR   SMR; A0A348B785; -.
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   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..344
FT                   /note="Sesquiterpene synthase 9"
FT                   /id="PRO_0000451391"
FT   MOTIF           88..92
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   MOTIF           224..232
FT                   /note="NSE/DTE motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         329..330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   SITE            85
FT                   /note="Plays a critical role in the stabilization of
FT                   intermediate cation"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   344 AA;  39636 MW;  B7AB46C44B93677A CRC64;
     MVRTRPTYIY LPDTAAGWPF PRTVNPYYEE TKAESEAWIS SLYPFDAYVQ KKFNACDFTL
     LASMAYPWLS KDHIRTGADL MMLFFVFDEY SDVASVKDAQ EMVDIVMDAL RNPHKPRPKD
     ENILGEIAKQ FWERGVKTAS APSARRFVDY FEGYLKSVVE QAQDREHNRI RSIAEYFDVR
     RLTVGARPSY ALMELGMNIP DEVWEDPAME IMAVCVTDMI ILDNDMLSWN VEQSRGDDAH
     NIVRIVMEAN KTDVASAMKW VEDYHNLLKK TFLDVYNSVP SWGPEVDAQV QEYARGLGNW
     VICNISWSFE SARYFGKEGR RIREERVVAI LDKPVLVGVL ESDA