STS1_STEHR
ID STS1_STEHR Reviewed; 369 AA.
AC P9WEW2;
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_73029 {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_73029 {ECO:0000303|PubMed:24166732};
GN ORFNames=STEHIDRAFT_73029;
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, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-53; ASP-111; GLU-116;
RP GLU-117 AND GLU-182.
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 (PubMed:26239156). In the presence of Co(2+) and Ni(2+) the
CC activity is retained and delta(6)-protoilludene is the major volatile
CC sesquiterpene produced (PubMed:26239156). In the presence of Ca(2+),
CC the major sesquiterpene produced switches to beta-elemene
CC (PubMed:26239156). {ECO:0000269|PubMed:26239156};
CC -!- ACTIVITY REGULATION: Ca(2+) switches the cyclization mechanism of
CC delta(6)-protoilludene synthase from 1,11 to 1,10 cyclization which
CC leads to the production of beta-elemene. {ECO:0000269|PubMed:26239156}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.52 uM for farnesyl diphosphate (FPP)
CC {ECO:0000269|PubMed:24166732};
CC KM=33.5 uM for Mg(2+) {ECO:0000269|PubMed:26239156};
CC KM=8.5 uM for Mn(2+) {ECO:0000269|PubMed:26239156};
CC KM=12.9 uM for Ca(2+) {ECO:0000269|PubMed:26239156};
CC KM=16.0 uM for Ni(2+) {ECO:0000269|PubMed:26239156};
CC KM=30.3 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}.
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DR EMBL; JH687380; EIM91236.1; -; Genomic_DNA.
DR RefSeq; XP_007299456.1; XM_007299394.1.
DR AlphaFoldDB; P9WEW2; -.
DR SMR; P9WEW2; -.
DR GeneID; 18806761; -.
DR KEGG; shs:STEHIDRAFT_73029; -.
DR OMA; ESRFMEN; -.
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..369
FT /note="Delta(6)-protoilludene synthase STEHIDRAFT_73029"
FT /id="PRO_0000451254"
FT MOTIF 107..111
FT /note="D(D/E)XX(D/E) motif"
FT /evidence="ECO:0000269|PubMed:26239156"
FT MOTIF 243..251
FT /note="NSE motif"
FT /evidence="ECO:0000269|PubMed:26239156"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 349..350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 104
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT MUTAGEN 53
FT /note="E->A: Does not affect cyclization in the presence of
FT Mg(2+) or Ca(2+), but impairs the activity in the presence
FT of Ni(2+) or Co(2+)."
FT /evidence="ECO:0000269|PubMed:26239156"
FT MUTAGEN 111
FT /note="D->A: Does not drastically affect cyclization in the
FT presence of Mg(2+), but impairs the activity in the
FT presence of Ca(2+)."
FT /evidence="ECO:0000269|PubMed:26239156"
FT MUTAGEN 116
FT /note="E->A: Does not drastically affect cyclization in the
FT presence of Mg(2+) or Co(2+), but severely affects the
FT activity in the presence of Ca(2+) and Ni(2+)."
FT /evidence="ECO:0000269|PubMed:26239156"
FT MUTAGEN 117
FT /note="E->A: Does not drastically affect cyclization in the
FT presence of Mg(2+) or Co(2+), but severely affects the
FT activity in the presence of Ca(2+) and Ni(2+)."
FT /evidence="ECO:0000269|PubMed:26239156"
FT MUTAGEN 182
FT /note="E->A: Does not drastically affect cyclization in the
FT presence of Mg(2+), but severely affects the activity in
FT the presence of Ca(2+), Ni(2+) or Co(2+)."
FT /evidence="ECO:0000269|PubMed:26239156"
SQ SEQUENCE 369 AA; 41515 MW; 0D88AC9A87349980 CRC64;
MAVATSVATP VPTPAYSAGR APAKEKKIYL PDTLAEWPWP RAINPHYAEA KEESQAWAAS
FNAFSPKAQH AFNRCDFNLL ASLAYPLATK HGCRSGCDLM NLFFVIDEYS DIAPVEEVRQ
QKDIVMDALR NPHKPRPEGE WVGGEVARQF WALTITNASA QSQKHFIETF DEYLDSVVQQ
AEDRSESRIR DIQSYIDVRR NTIGAKPSFA LLELDMDLPD EVLAHPTIQS LSLATIDMLC
LGNDIVSYNL EQARGDASHN IITIVMNELN LDVNGAMRWV GDFHKQLEKQ FFEAFNNLPK
WGNAELDAQI AVYCDGLGNW VRANDQWSFE SERYFGARGL EIMETKTLAM MPIQRTEALG
PQLVDDSIL
