ID   STS14_POSPM             Reviewed;         351 AA.
AC   A0A348B788;
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 14 {ECO:0000303|PubMed:30105900};
DE            EC=4.2.3.- {ECO:0000269|PubMed:30105900};
DE            EC=4.2.3.7 {ECO:0000269|PubMed:30105900};
DE   AltName: Full=Terpene cyclase 14 {ECO:0000303|PubMed:30105900};
GN   Name=STS-14 {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 pentalenene as a major product, as well as
CC       caryophyllene. {ECO:0000269|PubMed:30105900}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + pentalenene;
CC         Xref=Rhea:RHEA:18081, ChEBI:CHEBI:17251, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:175763; EC=4.2.3.7;
CC         Evidence={ECO:0000269|PubMed:30105900};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18082;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LC378434; BBD74526.1; -; mRNA.
DR   AlphaFoldDB; A0A348B788; -.
DR   SMR; A0A348B788; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050467; F:pentalenene 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..351
FT                   /note="Sesquiterpene synthase 14"
FT                   /id="PRO_0000451393"
FT   MOTIF           87..91
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   MOTIF           223..231
FT                   /note="NSE/DTE motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         87
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         328..329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   SITE            84
FT                   /note="Plays a critical role in the stabilization of
FT                   intermediate cation"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   351 AA;  40402 MW;  D5D2F96777C5313E CRC64;
     MSDQPKMIYL PETMANWPWP RYINPHYEEV KAESDAWFKG FKPFTKQSQV AFDKCDFGRL
     ASLAYPWASK EHLRTGCDLM NVFFMIDEYT DVECASVVRG MVDIVIDVIN NPHKPRPEGE
     SLLGEITRQF WERAIKAATP SSQKHFIEAF TDYLNSVVEQ AADRDNNHIR TVDSYLKTRR
     ENIGARPSYF PAELGLNLPD EAFYHPVVTE LSYNIAELII LDNDIASYNK EQATGDDRHN
     ILTIVMLQFN IDLEAAMTWV ASYHKDVENK FLDGMKKLPS FGPVVDKELE EYILALAIWP
     RTNDCWNFES GRYFGSKGLQ VQKTRYVPLL PKVKTDPTLK QKQVVVSLVD L