AGR1_AGRAE
ID AGR1_AGRAE Reviewed; 346 AA.
AC A0A5Q0QRJ3;
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=Sesquiterpene synthase Agr1 {ECO:0000303|PubMed:32233445};
DE EC=4.2.3.- {ECO:0000269|PubMed:32233445};
DE EC=4.2.3.125 {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 Agr1 {ECO:0000303|PubMed:32233445};
GN Name=Agr1 {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 alpha-muurolene,
CC gamma-muurolene, alpha-selinene, beta-selinene, delta-cadinene, alpha-
CC cadinol and delta-cadinol (PubMed:32233445). Delta-cadinene is the
CC major product of Agr1 (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 = alpha-muurolene + diphosphate;
CC Xref=Rhea:RHEA:33103, ChEBI:CHEBI:33019, ChEBI:CHEBI:64797,
CC ChEBI:CHEBI:175763; EC=4.2.3.125;
CC Evidence={ECO:0000269|PubMed:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33104;
CC Evidence={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 -!- 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; MN146024; QGA30877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q0QRJ3; -.
DR SMR; A0A5Q0QRJ3; -.
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..346
FT /note="Sesquiterpene synthase Agr1"
FT /id="PRO_0000451257"
FT MOTIF 98..102
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P0DL13"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 188
FT /ligand="substrate"
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 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 95
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 346 AA; 39574 MW; BFABF2FF030CAFFE CRC64;
MCASATRPQP SASNNVKKII LPDLVSHCTF KLRHNRHRKQ VTTETKKWLF KDGNLLGQKE
RAYHGLKCGL LTSMCYPDAG YPQLRVVNDF LTYLFHLDNL SDEMDNRGTT TTADEVLNSL
YHPHTWRSSA RVGKMTRDFY KRLVLTASPG AQQRFIETFD FFFQSVTQQA LDRASGVIPD
LESYISLRRD TSGCKPCWAM IEYANNLDIP DEVMDHPIIR SLGEATNDLV TWSNDIFSYS
VEQSKGHTHN MIPVVMYQEG LDLQAAVDFV GDMCRQSINR FVEEKARLPS WGPKIDQDVA
IYVQGLADWI VGSLHWSFET ERYFGKSGRQ VKASRIVDLL PRQRLP
