ID   STS8_POSPM              Reviewed;         342 AA.
AC   A0A348B784;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Delta(6)-protoilludene synthase 8 {ECO:0000303|PubMed:30105900};
DE            EC=4.2.3.135 {ECO:0000269|PubMed:30105900};
DE   AltName: Full=Terpene cyclase 8 {ECO:0000303|PubMed:30105900};
GN   Name=STS-08 {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 delta(6)-protoilludene.
CC       {ECO:0000269|PubMed:30105900}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = Delta(6)-protoilludene +
CC         diphosphate; Xref=Rhea:RHEA:34695, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:68655, ChEBI:CHEBI:175763; EC=4.2.3.135;
CC         Evidence={ECO:0000269|PubMed:30105900};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34696;
CC         Evidence={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; LC378430; BBD74522.1; -; mRNA.
DR   AlphaFoldDB; A0A348B784; -.
DR   SMR; A0A348B784; -.
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..342
FT                   /note="Delta(6)-protoilludene synthase 8"
FT                   /id="PRO_0000451390"
FT   MOTIF           93..97
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   MOTIF           217..225
FT                   /note="NSE/DTE motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         321..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   SITE            78
FT                   /note="Plays a critical role in the stabilization of
FT                   intermediate cation"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   342 AA;  39418 MW;  0F9115913C11B2E1 CRC64;
     MLYLPDTMSA WPWQRAINPY FNEVKAASNS WFKSFRAFSP ASQKAFDKCD FCLLAALAYP
     RARKEHLRTG CDLMNLFFVI DEYTDVEDAN VCRDMVDIVI DALRRPHDPR PEGEVVLGEI
     ARQFWARAIE TASPTSQRRF LETFIAYLES VVLQAADRDC DAEHTVQTYL AQRRDNIGSY
     PSYAVLELAL DIPDDIFYHP AMNELSLYAT EMLIIDNDLV SYNREQASGD TNNILFVIMR
     QFNCSLDHAM AWAAAYHSQL EARFMDAFKR MPSWGLEIDS QVEEYCQGIA NWPRGNDCWS
     FESGRYFGDK GREVQKTRCV PLLPKKERDT SLRQQDVVIT SL