ID   AGR2_AGRAE              Reviewed;         389 AA.
AC   A0A5Q0QNJ2;
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=viridiflorene synthase Agr2 {ECO:0000303|PubMed:32233445};
DE            EC=4.2.3.88 {ECO:0000269|PubMed:32233445};
DE   AltName: Full=Sesquiterpene synthase Agr2 {ECO:0000303|PubMed:32233445};
DE   AltName: Full=Terpene cyclase Agr2 {ECO:0000303|PubMed:32233445};
DE   Flags: Precursor;
GN   Name=Agr2 {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 viridiflorene. {ECO:0000269|PubMed:32233445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene;
CC         Xref=Rhea:RHEA:31811, ChEBI:CHEBI:33019, ChEBI:CHEBI:63444,
CC         ChEBI:CHEBI:175763; EC=4.2.3.88;
CC         Evidence={ECO:0000269|PubMed:32233445};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31812;
CC         Evidence={ECO:0000269|PubMed:32233445};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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; MN146025; QGA30878.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5Q0QNJ2; -.
DR   SMR; A0A5Q0QNJ2; -.
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; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..389
FT                   /note="viridiflorene synthase Agr2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5024343511"
FT   MOTIF           128..132
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL13"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         376..377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ   SEQUENCE   389 AA;  44434 MW;  D12C665F19646DA3 CRC64;
     MVWDFVLSLF HSLLAAFQTL TSWLTGSFLF NNKMAPAPNP APVTFILPDL EKTFNSLPDD
     GLNPHHDVAC AESREWFAKY NKKVLGAQMQ EFFRRCKFEL ITSYTYPYVD KEGLRATMDW
     HNILWFFDEV TDTETGKDAH KSAIITIRTL REPDFDDGSS LCRMVRDFRL SHLSRAGPEC
     TRRFLEHCDV AFHAGAVEAE LREKGEVLSI EGYLKLRRET SGARTCFDMA EYLMDIDLPQ
     DMYDDPVFQK GYIAALDLIF LANDLYSYNM EQAKGHNGAN VLTVVMKETK LNLQSAADYV
     GVLCEKLIKQ FQEAKSTLEN RLAKEKNPAK AAALKDAIRS LVGYGHWVRG NVEWSFETER
     YFGKKNKEIK KSRVVTLTPT NSVNRALKA