AGR6_AGRAE
ID AGR6_AGRAE Reviewed; 659 AA.
AC A0A5Q0QN66;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 03-AUG-2022, entry version 11.
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=Agr6 {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:0000250|UniProtKB:I3ZNU9};
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.
CC {ECO:0000250|UniProtKB:I3ZNU9}.
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DR EMBL; MN146029; QGA30882.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q0QN66; -.
DR SMR; A0A5Q0QN66; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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 Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
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..659
FT /note="Delta(6)-protoilludene synthase"
FT /id="PRO_0000451260"
FT REGION 528..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..95
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P0DL13"
FT COMPBIAS 531..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 235
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 88
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 659 AA; 72432 MW; 258F15ADEAC095E9 CRC64;
MPGSANWTAD RFYIPDTLAN WPWPRAINPA YEECKAASAA WCEKYGAFSA RAQKAFNLCD
FNLLASLAYA GLPADVNRVG CDLMNLFFVV DEHTDAMDAR SVQDWVDIVV DALHHPHTPR
PAGEPKVGEI ARTFWENGIK CMGPTAQRRF VETFTTYLQS VVTQAQDRDK HLFRDVDSYM
EVRRDTIGAK PSFALLEHDM ELPDDVFYHP LLEKLREWAI DMLILGNDLC SYNVEQSRGD
DGHNIIRLAM LQENTNVHGA LRFVSKMHDD LAEKFLSNYQ GMPSFTPQID AWVTRYIDGL
GNWVRANDSW SFESWRYFKG DVLRVQAERW VELLPPAPKD ELTSSIPPES RWIKPAVEPS
RARPNNVGIV ALDTYTPTSE DDFQTLAVKT VSSLLSKYNI NPVSVGRLDI CIERAADPYI
IYALRDAFAS AGNTDVEAIV SSSKSVVGLF NAINWVESSS WDGRYAIVFA GDLSSGVSAA
LVGPDAPIVV EPTRGTYLGD PIASTDEAQG SYIDSLFQSY SHYRKKHPQF SKTSGAPNGA
HTPTTTNGSI KSNGFVSGDT NGHANGNGHV QTRSSTPSSS SSSTSSPSFD YMILHDRHGK
IPTGAGSIYL GLASLITDIA PETLAGKSIG VFGFANSTST FFGIRVAGDC SVICKQLQA
