STS2_POSPM
ID STS2_POSPM Reviewed; 338 AA.
AC A0A348B780;
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=Sesquiterpene synthase 2 {ECO:0000303|PubMed:30105900};
DE EC=4.2.3.- {ECO:0000269|PubMed:30105900};
DE EC=4.2.3.125 {ECO:0000269|PubMed:30105900};
DE EC=4.2.3.126 {ECO:0000269|PubMed:30105900};
DE EC=4.2.3.127 {ECO:0000269|PubMed:30105900};
DE EC=4.2.3.133 {ECO:0000269|PubMed:30105900};
DE AltName: Full=Terpene cyclase 2 {ECO:0000303|PubMed:30105900};
GN Name=STS-02 {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 alpha-copaene,
CC beta-copaene, beta-elemene, alpha-muurolene, gamma-muurolene and delta-
CC cadinene. {ECO:0000269|PubMed:30105900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate;
CC Xref=Rhea:RHEA:33991, ChEBI:CHEBI:10221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.133;
CC Evidence={ECO:0000269|PubMed:30105900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33992;
CC Evidence={ECO:0000269|PubMed:30105900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate;
CC Xref=Rhea:RHEA:33111, ChEBI:CHEBI:33019, ChEBI:CHEBI:64799,
CC ChEBI:CHEBI:175763; EC=4.2.3.127;
CC Evidence={ECO:0000269|PubMed:30105900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33112;
CC Evidence={ECO:0000269|PubMed:30105900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate;
CC Xref=Rhea:RHEA:33103, ChEBI:CHEBI:33019, ChEBI:CHEBI:64797,
CC ChEBI:CHEBI:175763; EC=4.2.3.125;
CC Evidence={ECO:0000269|PubMed:30105900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33104;
CC Evidence={ECO:0000269|PubMed:30105900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene;
CC Xref=Rhea:RHEA:33107, ChEBI:CHEBI:33019, ChEBI:CHEBI:64798,
CC ChEBI:CHEBI:175763; EC=4.2.3.126;
CC Evidence={ECO:0000269|PubMed:30105900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33108;
CC Evidence={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 -!- 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; LC378426; BBD74518.1; -; mRNA.
DR AlphaFoldDB; A0A348B780; -.
DR SMR; A0A348B780; -.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IEA:UniProtKB-EC.
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..338
FT /note="Sesquiterpene synthase 2"
FT /id="PRO_0000451387"
FT MOTIF 93..97
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:30105900"
FT MOTIF 228..236
FT /note="NSE/DTE motif"
FT /evidence="ECO:0000305|PubMed:30105900"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 182
FT /ligand="substrate"
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 236
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 90
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 338 AA; 38419 MW; 004F5BC87970AFF7 CRC64;
MSSSVSSTSA PTKIVIPDLV SHCTIPVRCN RHWKQASVES KRWLFRGGNL SDRKRDAFHG
LKAGYLTSMC YPLAGYPQLR VSCDFMNYLF HLDNISDEMN DRGTHGTAVS VLDALYQPHM
HPTSRVGKMT KDYWVRLIQT ASPGAQQRFI ETFDMFFQAV TQQAMDRANG VIPDLESYIA
IRRDTSGCKP CWALIEYANN LDLPWEIMDH PIIRGLGEAA NDLVTWSNDI FSYNVEQSKG
DTHNMIVVVQ NQQGLDLQSA VNFVGDLCKQ SIDRFHYLRE NLPSWGPELD REVEIYVDGL
ADWITGSLKW SFESERYFGK AGLEVKKTRV VALLPRRA
