ID   AGR5_AGRAE              Reviewed;         430 AA.
AC   A0A5Q0QSI8;
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 Agr5 {ECO:0000303|PubMed:32233445};
DE            EC=4.2.3.- {ECO:0000269|PubMed:32233445};
DE            EC=4.2.3.88 {ECO:0000269|PubMed:32233445};
DE   AltName: Full=Terpene cyclase Agr5 {ECO:0000303|PubMed:32233445};
DE   Flags: Precursor;
GN   Name=Agr5 {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 and viridiflorol.
CC       {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         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.
CC       {ECO:0000269|PubMed:32233445}.
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DR   EMBL; MN146028; QGA30881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5Q0QSI8; -.
DR   SMR; A0A5Q0QSI8; -.
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   Glycoprotein; Lyase; Magnesium; Metal-binding; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..430
FT                   /note="Sesquiterpene synthase Agr5"
FT                   /id="PRO_5024438505"
FT   MOTIF           176..180
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL13"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         417..418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   430 AA;  48034 MW;  0ABE05DFAE39A4F7 CRC64;
     MASSLLEPSL AAIALVILLA SVSLSRKKRP AAPEPQGLSV LGNLFDIPKR ASSIIYLALG
     KPYNTLTKRA VSQLQGYTPG SHIDATSHSP RVFRLPNLEE TFSVFPDHGL NPNYTSARTD
     SRAWINQYTK VVCGPKMVAF MNNCEFELSN SHCYPYAGYK GLKATMDLTN ILWLYDEYTD
     TGSGAEAVKA AGIVARALRE PDYDDGTWVC RMMKSFKQNH IDKAGPGVAR RFIDNFCNYV
     EVVGREAELR EKNEVLDIPN YVTFRRETSA VRTCFDLVEY CLDLDLPQYV HDDPVFISGY
     NAGMDLVFWA NDLVSYNMEQ SKGHSGANVV TVIMKSKGVD LQTAVDFLGG YCEALTAQLL
     EAKRILQARS DAAYSRDVVR LMDAFGDWVR GNVAWSFETE RYFGKENKRV KETLLVELKE
     PFVGALALKE