AGR4_AGRAE
ID AGR4_AGRAE Reviewed; 342 AA.
AC A0A5Q0QP64;
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=Bifunctional terpene synthase Agr4 {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=4.2.3.127 {ECO:0000269|PubMed:32233445};
DE EC=4.2.3.15 {ECO:0000269|PubMed:32233445};
DE AltName: Full=Terpene cyclase Agr4 {ECO:0000303|PubMed:32233445};
GN Name=Agr4 {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-copaene,
CC alpha-cubebene, cadina-1(6),4-diene, gamma-muurolene, delta-cadinene,
CC epizonarene, epicubenol and cubenol (PubMed:32233445). Agr4 is also
CC able to use the monoterpene precursor geranyl diphosphate (GPP) as
CC substrates to synthesize the monoterpene beta-myrcene
CC (PubMed:32233445). Delta-cadinene is the major product of Agr4
CC (PubMed:32233445). {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 -!- 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 = beta-copaene + diphosphate;
CC Xref=Rhea:RHEA:33111, ChEBI:CHEBI:33019, ChEBI:CHEBI:64799,
CC ChEBI:CHEBI:175763; EC=4.2.3.127;
CC Evidence={ECO:0000269|PubMed:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33112;
CC Evidence={ECO:0000269|PubMed:32233445};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
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; MN146027; QGA30880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q0QP64; -.
DR SMR; A0A5Q0QP64; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
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..342
FT /note="Bifunctional terpene synthase Agr4"
FT /id="PRO_0000451259"
FT MOTIF 87..91
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P0DL13"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 87
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 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 324..325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 84
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 342 AA; 38560 MW; 18A9AE72BCCF0250 CRC64;
MSALPSQFKL PDLLSTCPLK DGTNPAYKKA AAESRAWIGS YNMFADRKRA FFIQGQNELL
CSHVYCYAGY EQLRTTCDFV NLLFVVDEVS DEQSGEDARA TGQVFVNAMK YADWHDGSKL
AKLTKDFRVR FLRLAGPKNV ARFVALCESY TACVGKEAEL RESGQVLGVK EFIPLRRQNS
AVLLCFSLVE YILGIDLDDE VYRDENFLNA YWAACDHVCW ANDVYSYDME QSKGLSNNNI
VTVLMEENHT SLQDTSDYIG EKCAEFVQIY LTSKKRLSPS LGPDAALFLE SIGSWMVGNL
AWSFETSRYF GSRHLEVKET GIVILRPREL PEDGSSSDSD EE
