STS10_POSPM
ID STS10_POSPM Reviewed; 336 AA.
AC B8PD44;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Sesquiterpene synthase 10 {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=4.2.3.128 {ECO:0000269|PubMed:30105900};
DE EC=4.2.3.133 {ECO:0000269|PubMed:30105900};
DE AltName: Full=Terpene cyclase 10 {ECO:0000303|PubMed:30105900};
GN Name=STS-10 {ECO:0000303|PubMed:30105900}; ORFNames=POSPLDRAFT_98072;
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], 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R;
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC -!- FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl
CC diphosphate (FPP) to various sesquiterpenes, including alpha-cubebene,
CC beta-cubebene, sativene, cyclosativene, sesquisabinene, alpha-copaene,
CC beta-copaene, cadina-1(6),4-diene, alpha-muurolene, gamma-muurolene,
CC bicyclosesquiphellandrene, allo-aromadendr-9-en, epi-cubebol, cubebol
CC and delta-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 = 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 = beta-cubebene + diphosphate;
CC Xref=Rhea:RHEA:32019, ChEBI:CHEBI:10363, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.128;
CC Evidence={ECO:0000269|PubMed:30105900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32020;
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 -!- 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; LC378432; BBD74524.1; -; mRNA.
DR EMBL; EQ966319; EED81184.1; -; Genomic_DNA.
DR RefSeq; XP_002473599.1; XM_002473554.1.
DR AlphaFoldDB; B8PD44; -.
DR SMR; B8PD44; -.
DR EnsemblFungi; EED81184; EED81184; POSPLDRAFT_98072.
DR KEGG; ppl:POSPLDRAFT_98072; -.
DR HOGENOM; CLU_042538_2_1_1; -.
DR InParanoid; B8PD44; -.
DR OMA; AMEHWVI; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
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; Reference proteome.
FT CHAIN 1..336
FT /note="Sesquiterpene synthase 10"
FT /id="PRO_0000451392"
FT MOTIF 87..91
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:30105900"
FT MOTIF 222..230
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 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 327..328
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 336 AA; 38275 MW; FAECA51E910FCAD2 CRC64;
MPSTPRQFVL PDLFPLVPFK GSTNPHYVKA AAESSAWINS YNVFTDRKRA FFIQGSNELL
VSHTYPYAGY EQFRTCCDFV NLLFVVDEVS DEQNGKDARH TGNVYLKAMR DPEWNDGSVL
AKMTKEFRAR LLQYAGPGCY ARFLKHCEDY VEAVAKEAEY RECGVVLDMA SFETLRRENS
AIRLCFGLFE YCLGVDLPEY VFEDPTFMTL YWAAADMVCW SNDVYSYNME QAKGIGGNNI
VTVLMQAKGI DVQAACDAVG EHCKLLMERY LDAKEKLPSW GPSVDDAVAG YVQAMEHWII
GNLEWSFETQ RYFGAVHAEV KATRVVMLRP REIDED
