PROS_HYPSF
ID PROS_HYPSF Reviewed; 327 AA.
AC A0A0D2L718;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Delta(6)-protoilludene synthase HYPSUDRAFT_138665 {ECO:0000303|PubMed:32233445};
DE EC=4.2.3.135 {ECO:0000269|PubMed:32233445};
DE AltName: Full=Sesquiterpene synthase HYPSUDRAFT_138665 {ECO:0000303|PubMed:32233445};
DE AltName: Full=Terpene cyclase HYPSUDRAFT_138665 {ECO:0000303|PubMed:32233445};
GN ORFNames=HYPSUDRAFT_138665;
OS Hypholoma sublateritium (strain FD-334 SS-4).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Strophariaceae; Hypholoma.
OX NCBI_TaxID=945553;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-334 SS-4;
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=32233445; DOI=10.1021/acschembio.0c00155;
RA Zhang C., Chen X., Orban A., Shukal S., Birk F., Too H.P., Ruehl M.;
RT "Agrocybe aegerita serves as a gateway for identifying sesquiterpene
RT biosynthetic enzymes in higher fungi.";
RL ACS Chem. Biol. 15:1268-1277(2020).
CC -!- FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl
CC diphosphate (FPP) to delta(6)-protoilludene.
CC {ECO:0000269|PubMed:32233445}.
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:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34696;
CC Evidence={ECO:0000269|PubMed:32233445};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:32233445};
CC -!- DOMAIN: The DDXXD motif is important for the catalytic activity,
CC presumably through binding to Mg(2+). {ECO:0000269|PubMed:32233445}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; KN817547; KJA22852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2L718; -.
DR SMR; A0A0D2L718; -.
DR EnsemblFungi; KJA22852; KJA22852; HYPSUDRAFT_138665.
DR OMA; ESRFMEN; -.
DR OrthoDB; 1143139at2759; -.
DR Proteomes; UP000054270; 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 Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..327
FT /note="Delta(6)-protoilludene synthase HYPSUDRAFT_138665"
FT /id="PRO_0000451271"
FT MOTIF 79..83
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P0DL13"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 320..321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 76
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 327 AA; 37519 MW; C89A56E4ED0AE568 CRC64;
MALSNSNSTT ATVTLPDTLR FWPWQRHINP HYSACKKASS EWCESFKAFS PQAQRAFNKC
DFNGCRIGCD LMNLFFIIDE HTDIASAETA RTQANIIMEA IRDPEMPRSE NEWVGGKAAQ
QFWLNATKSA TPSAHRRFID AFQMYMDAVV QQAADRSKNY VRDIDDYFVV RRDTIGAKPS
FAICELYLNL PDSVMEHPVI MKLTELCIDV IIIGNDLCSY KVEHEHGDDG HNLITVVMNQ
FKITPQEAMN YISDLHDKLA VQFLDEWKNI PTFGGPLDLE VRTYCHGLGN WVRANDSWSF
ESERYFGKRG IEIQTTRQIE MNIQSHL
