ID   STS29_POSPM             Reviewed;         340 AA.
AC   A0A348B794;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Terpene synthase 29 {ECO:0000303|PubMed:30105900};
DE            EC=4.2.3.- {ECO:0000269|PubMed:30105900};
DE   AltName: Full=Terpene cyclase 29 {ECO:0000303|PubMed:30105900};
GN   Name=STS-29 {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 terpene scaffold whose chemical
CC       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 trichodiene synthase family. {ECO:0000305}.
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DR   EMBL; LC378440; BBD74532.1; -; mRNA.
DR   AlphaFoldDB; A0A348B794; -.
DR   SMR; A0A348B794; -.
DR   GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
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; IPR024652; Trichodiene_synth.
DR   Pfam; PF06330; TRI5; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..340
FT                   /note="Terpene synthase 29"
FT                   /id="PRO_0000451376"
FT   MOTIF           132..138
FT                   /note="DDXXXXD motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   MOTIF           257..265
FT                   /note="NSE/DTE motif"
FT                   /evidence="ECO:0000305|PubMed:30105900"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13513"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P13513"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13513"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13513"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P13513"
SQ   SEQUENCE   340 AA;  38203 MW;  AD90A6A8D225516C CRC64;
     MSAVTQVVET AIGCVIPSCI EFGSSMRIAT SLGSPSVTQS PCVNRDVEDI ARTARESIRF
     FLAELSIECV PYTQDPALEA QVASATRCWP DRERLAPHIR TGIVIAATAY AHNSLATRTL
     IALYTAIGVA LDEPDILESA NAIGFHHSLC TETSERPSAI LDEWRRILAR MWDHFPRFGA
     SCILTSTLQF LNMTMLENET KGKVLNRTAM PFVEYRRMTD GFPEVYTAFI WEKGRFPDVQ
     VYMQAIPNAM RFINFGNDIL SFYKEEAAGE TGTYIHDRAR LTGLSSVETL REVVEETVSA
     WRQVCEILGE GIARDAWNSF VRGYVTFHVH NPRYRLSELL