ID   AGR7_AGRAE              Reviewed;         387 AA.
AC   A0A5Q0QNH9;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Delta(6)-protoilludene synthase {ECO:0000303|PubMed:32233445};
DE            EC=4.2.3.135 {ECO:0000269|PubMed:32233445};
DE   AltName: Full=Terpene cyclase Agr6 {ECO:0000303|PubMed:32233445};
GN   Name=Agr7 {ECO:0000303|PubMed:32233445};
OS   Agrocybe aegerita (Black poplar mushroom) (Agaricus aegerita).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Bolbitiaceae; Cyclocybe.
OX   NCBI_TaxID=1973307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, AND CATALYTIC
RP   ACTIVITY.
RC   STRAIN=AAE3_05024;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAE3_05024;
RX   PubMed=29334897; DOI=10.1186/s12864-017-4430-y;
RA   Gupta D.K., Ruehl M., Mishra B., Kleofas V., Hofrichter M., Herzog R.,
RA   Pecyna M.J., Sharma R., Kellner H., Hennicke F., Thines M.;
RT   "The genome sequence of the commercially cultivated mushroom Agrocybe
RT   aegerita reveals a conserved repertoire of fruiting-related genes and a
RT   versatile suite of biopolymer-degrading enzymes.";
RL   BMC Genomics 19:48-48(2018).
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; MN146030; QGA30883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5Q0QNH9; -.
DR   SMR; A0A5Q0QNH9; -.
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.
FT   CHAIN           1..387
FT                   /note="Delta(6)-protoilludene synthase"
FT                   /id="PRO_0000451261"
FT   MOTIF           90..94
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL13"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         90
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         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         234
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            87
FT                   /note="Plays a critical role in the stabilization of
FT                   intermediate cation"
FT                   /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ   SEQUENCE   387 AA;  44849 MW;  DACE2F440966C55C CRC64;
     MSFFKSSQPT IYIPDTLRNW PWPREINPHY EECKRESAAW VEKFGAFSAK AQKAFNKCDF
     NLLASLAWSR VNRDGCRIGC DLMNLFFVFD EWSDVSDAEE TRRMADIIMD ALYDPHKPRP
     TGEWVGGEVT RQYWLNAIRT ATPSAQKRFI KAFKLYTDSV VQQSADRDKH LIRDIDSYFE
     VRRDTIGAKP SFAINEVHMN LPDYVMEHPV IKNLTAYCID MLCIGNDLCS YNVEQSRGDD
     GHNLVTIVMH QLNLDVQGAF DWIGKLHDEL VDKFLEEYKN VPTFKDKQVT KECAEYAFGL
     GNWVRGNDQW SFESERYFRK DGMRVLTERT VVLLPKKREP PPKPLDEDPI YSALPWWGWT
     ALFGFLATAF TFSARQLSTR ISANLIA