STS3_STEHR
ID STS3_STEHR Reviewed; 351 AA.
AC P9WEW0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Delta(6)-protoilludene synthase STEHIDRAFT_25180 {ECO:0000303|PubMed:24166732};
DE EC=4.2.3.- {ECO:0000269|PubMed:26239156};
DE EC=4.2.3.135 {ECO:0000269|PubMed:24166732, ECO:0000269|PubMed:26239156};
DE EC=4.2.3.198 {ECO:0000269|PubMed:26239156};
DE AltName: Full=Terpene cyclase STEHIDRAFT_25180 {ECO:0000303|PubMed:24166732};
GN ORFNames=STEHIDRAFT_25180;
OS Stereum hirsutum (strain FP-91666) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Stereaceae; Stereum.
OX NCBI_TaxID=721885;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP-91666;
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24166732; DOI=10.1002/cbic.201300349;
RA Quin M.B., Flynn C.M., Wawrzyn G.T., Choudhary S., Schmidt-Dannert C.;
RT "Mushroom hunting by using bioinformatics: application of a predictive
RT framework facilitates the selective identification of sesquiterpene
RT synthases in basidiomycota.";
RL ChemBioChem 14:2480-2491(2013).
RN [3]
RP FUNCTION, DOMAIN, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=26239156; DOI=10.1002/cbic.201500308;
RA Quin M.B., Michel S.N., Schmidt-Dannert C.;
RT "Moonlighting metals: insights into regulation of cyclization pathways in
RT fungal delta(6)-protoilludene sesquiterpene synthases.";
RL ChemBioChem 16:2191-2199(2015).
CC -!- FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl
CC diphosphate (FPP) to delta(6)-protoilludene (PubMed:24166732,
CC PubMed:26239156). In presence of Ca(2+), a significant switch from 1,11
CC to a dual 1,11/1,10 cyclization occurs, producing beta-elemene as the
CC major product, with lower levels of delta(6)-protoilludene and (E)-
CC beta-caryophyllene, and traces of beta-selinene and alpha-selinene
CC (PubMed:26239156). {ECO:0000269|PubMed:24166732,
CC ECO:0000269|PubMed:26239156}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = Delta(6)-protoilludene +
CC diphosphate; Xref=Rhea:RHEA:34695, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:68655, ChEBI:CHEBI:175763; EC=4.2.3.135;
CC Evidence={ECO:0000269|PubMed:24166732, ECO:0000269|PubMed:26239156};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34696;
CC Evidence={ECO:0000269|PubMed:24166732, ECO:0000269|PubMed:26239156};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-selinene + diphosphate;
CC Xref=Rhea:RHEA:47052, ChEBI:CHEBI:33019, ChEBI:CHEBI:59961,
CC ChEBI:CHEBI:175763; EC=4.2.3.198;
CC Evidence={ECO:0000269|PubMed:26239156};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47053;
CC Evidence={ECO:0000269|PubMed:26239156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24166732};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24166732};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:24166732};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:24166732};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:24166732};
CC Note=Mg(2+) and Mn(2+) are more tightly associated with the active site
CC motifs (D(D/E)XX(D/E) and NSE) and thus lead to more efficient removal
CC of PPi. {ECO:0000269|PubMed:26239156};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.02 uM for farnesyl diphosphate (FPP)
CC {ECO:0000269|PubMed:24166732};
CC KM=17.3 uM for Mg(2+) {ECO:0000269|PubMed:26239156};
CC KM=10.6 uM for Mn(2+) {ECO:0000269|PubMed:26239156};
CC KM=9.8 uM for Ca(2+) {ECO:0000269|PubMed:26239156};
CC KM=35.2 uM for Ni(2+) {ECO:0000269|PubMed:26239156};
CC KM=17.3 uM for Co(2+) {ECO:0000269|PubMed:26239156};
CC -!- DOMAIN: The 2 conserved active-site motifs D(D/E)XX(D/E) and NSE are
CC required for coordinating the divalent metal ions that stabilize the
CC PPi moiety of the substrate. {ECO:0000269|PubMed:26239156}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EIM88705.1; Type=Erroneous gene model prediction; Evidence={ECO:0000269|PubMed:24166732};
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DR EMBL; JH687382; EIM88705.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_007301467.1; XM_007301405.1.
DR AlphaFoldDB; P9WEW0; -.
DR SMR; P9WEW0; -.
DR GeneID; 18804339; -.
DR KEGG; shs:STEHIDRAFT_25180; -.
DR Proteomes; UP000053927; Unassembled WGS sequence.
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 Calcium; Cobalt; Lyase; Magnesium; Manganese; Metal-binding; Nickel;
KW Reference proteome.
FT CHAIN 1..351
FT /note="Delta(6)-protoilludene synthase STEHIDRAFT_25180"
FT /id="PRO_0000451256"
FT MOTIF 89..93
FT /note="D(D/E)XX(D/E) motif"
FT /evidence="ECO:0000269|PubMed:26239156"
FT MOTIF 225..233
FT /note="NSE motif"
FT /evidence="ECO:0000269|PubMed:26239156"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 331..332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 86
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 351 AA; 40486 MW; D09AFC1D2771B08E CRC64;
MTVVDSPQRF YIPNCLEYWP WPRHINPHYQ EVKKASAAWA ESFGAFNPKA QHAYNACDFN
LLASLAYPLE SEERLRTGCD LMNMFFVFDE YSDVSSPKDV IQQAAIIMDA LRNPYAPRPD
DEWVGGEVTR QFWKRAIKTA TAGAQRRFID AFESYTQSVV QQAKDRHHGF IRDVDSYLEM
RRETIGAKPS FVVLQMDMTL PDEVLAHPVI QQLSALSTDM ICLGNDICSY NVEQARGDDL
HNIITIAMNQ FDIDIAGAMD WVVKYHAKLE RKFLYLYNNG LPSWGKELDP QVERYVCGLG
NWVRASDQWG FESERYFGKK GKEIFKRRWV NLMQPERAQD IGPTLVDGTR L
