ID   STS6_POSPM              Reviewed;         340 AA.
AC   A0A348B782;
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=Sesquiterpene synthase 6 {ECO:0000303|PubMed:30105900};
DE            EC=4.2.3.- {ECO:0000269|PubMed:30105900};
DE            EC=4.2.3.100 {ECO:0000269|PubMed:30105900};
DE   AltName: Full=Terpene cyclase 6 {ECO:0000303|PubMed:30105900};
GN   Name=PpSTS-06 {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 various sesquiterpenes, including bicycloelemene,
CC       alpha-gurjunene, 9-epi-caryophylene, bicyclosesquiphellandrene,
CC       bicyclogermacrene and delta-cadinene. {ECO:0000269|PubMed:30105900}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate;
CC         Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564,
CC         ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:30105900};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557;
CC         Evidence={ECO:0000269|PubMed:30105900};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = bicyclogermacrene +
CC         diphosphate; Xref=Rhea:RHEA:31999, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:63709, ChEBI:CHEBI:175763; EC=4.2.3.100;
CC         Evidence={ECO:0000269|PubMed:30105900};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32000;
CC         Evidence={ECO:0000269|PubMed:30105900};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:30105900};
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; LC378428; BBD74520.1; -; mRNA.
DR   AlphaFoldDB; A0A348B782; -.
DR   SMR; A0A348B782; -.
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..340
FT                   /note="Sesquiterpene synthase 6"
FT                   /id="PRO_0000451389"
FT   MOTIF           90..94
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   MOTIF           229..237
FT                   /note="NSE/DTE motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         332..333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   SITE            87
FT                   /note="Plays a critical role in the stabilization of
FT                   intermediate cation"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   340 AA;  38697 MW;  3DEF0495F34A1E81 CRC64;
     MTVIADTSRC FILPDLISYC QFPLRCNPHR DAAQSSTSWL INNYPGMSPE QLVEVRRLDA
     DTLASYCYPD CDVERLRVAS DFLAILFHLD DITDTMEEGG TEQLEGTIMD AFRSEGKLDQ
     REDEPRVRVP AKDLWTRFIR NAKPCVQTRL RDNIALFFKT AREEARDRER GVLLDLESYI
     NMRRGTSACL SCFALTEYSI GIELPQYVVD DPIVQALNQS ANDLVSWSND IYSFNNEQAH
     GIHNMIVILM KSQGLGMQDA IDYVSDLFKQ TIDGFMENTQ LLPSWGAAVD ADVRLYVQGL
     QDWVVGNLHW SFATERYFGK RGAEIKATRV VELLPKKPVS