ID   TERS_GALM3              Reviewed;         345 AA.
AC   A0A067SEC9;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Sesquiterpene synthase GALMADRAFT_104215 {ECO:0000303|PubMed:32233445};
DE            EC=4.2.3.- {ECO:0000269|PubMed:32233445};
DE   AltName: Full=Terpene cyclase GALMADRAFT_104215 {ECO:0000303|PubMed:32233445};
GN   ORFNames=GALMADRAFT_104215;
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88;
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
RN   [2]
RP   FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
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).
CC   -!- FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl
CC       diphosphate (FPP) to beta-gurjunene. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL142403; KDR69261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067SEC9; -.
DR   SMR; A0A067SEC9; -.
DR   EnsemblFungi; KDR69261; KDR69261; GALMADRAFT_104215.
DR   HOGENOM; CLU_042538_2_1_1; -.
DR   OrthoDB; 1143139at2759; -.
DR   Proteomes; UP000027222; Unassembled WGS sequence.
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; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Sesquiterpene synthase GALMADRAFT_104215"
FT                   /id="PRO_0000451268"
FT   MOTIF           91..95
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL13"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         180
FT                   /ligand="substrate"
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         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         332..333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ   SEQUENCE   345 AA;  39447 MW;  E351940538776F6E CRC64;
     MNTTTRTFYL PRLEDTFSVF PDNGLNPHYA ECRIQSQAWI DKYYKIVCGP KMRAYMDHCK
     FELITAYTYP YASSDGLRKT MDLANILWLY DEFTDTLSGK DATNAAAIVI RTLRERDFDD
     GSWICHMMRD FYAAHIEKFG PNVSRRFIDH FCQYVEGTGT EAKHREKDHV LDINAYIIMR
     RAASAVLTAF DLAEYCLGID LPQYVHDDPA FISGYNAGLD LVFLDNDLFS YDMEQAKGHC
     TTNIITVVMK SKRIDLQSAF DFTAGYCESL TQQLIAAQIS LASRTDPVFS NNAVKCLEAI
     ANWVKGSDGW SFATERYFGK QNVIVKETRA VEMRKSFQDI AVLKE