AGR8_AGRAE
ID AGR8_AGRAE Reviewed; 353 AA.
AC A0A5Q0QMX1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Sesquiterpene synthase Agr8 {ECO:0000303|PubMed:32233445};
DE EC=4.2.3.- {ECO:0000269|PubMed:32233445};
DE EC=4.2.3.126 {ECO:0000269|PubMed:32233445};
DE EC=4.2.3.198 {ECO:0000269|PubMed:32233445};
DE AltName: Full=Terpene cyclase Agr8 {ECO:0000303|PubMed:32233445};
GN Name=Agr8 {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 various sesquiterpenes, including beta-elemene,
CC gamma-muurolene, alpha-selinene, beta-selinene, beta-cadinene, delta-
CC cadinene and alpha-cadinol. {ECO:0000269|PubMed:32233445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene;
CC Xref=Rhea:RHEA:33107, ChEBI:CHEBI:33019, ChEBI:CHEBI:64798,
CC ChEBI:CHEBI:175763; EC=4.2.3.126;
CC Evidence={ECO:0000269|PubMed:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33108;
CC Evidence={ECO:0000269|PubMed:32233445};
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:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47053;
CC Evidence={ECO:0000269|PubMed:32233445};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = delta-cadinene + diphosphate;
CC Xref=Rhea:RHEA:56556, ChEBI:CHEBI:33019, ChEBI:CHEBI:140564,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56557;
CC Evidence={ECO:0000269|PubMed:29334897};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|RuleBase:RU366034};
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; MN146031; QGA30884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q0QMX1; -.
DR SMR; A0A5Q0QMX1; -.
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..353
FT /note="Sesquiterpene synthase Agr8"
FT /id="PRO_0000451262"
FT MOTIF 82..86
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P0DL13"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 325..326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 79
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 353 AA; 40511 MW; 4B71E845FD465F8B CRC64;
MSEQQYTLPD LLQNWPWNRH LSPYYEEAKR ESSAWVESFK PFDQDGQRAF DAYLLASLTY
SHGSREFVRL GCDLMNFYFV YDEYTDVSDS AVADRLANIV IDAMRNPENS SQSGDHLLGK
MTKHFWTRAL AMAPAGSPCF EHFITTSETY LRAVTQEAED RANKRVRKVD DYLRLRRDTC
GARPTLALIE FGLNLPNEVV RHPSLVALTE AAVDLIILVN DMHSYVRELS CGHENHNLIT
AIMLEHRLNR QDAFHWLGSH CSRVVDQFLS DLDELPSWGE PTDSGVRDYI NGLGQWVRGN
DDWSTESKRY YGEDGETIRQ ERLVTTRSGE SNYIKFGQVG VQDSVRIQPI EAN
