ID   TERS_SPHS4              Reviewed;         347 AA.
AC   A0A0C9VD04;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Sesquiterpene synthase M422DRAFT_47084 {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 M422DRAFT_47084 {ECO:0000303|PubMed:32233445};
GN   ORFNames=M422DRAFT_47084;
OS   Sphaerobolus stellatus (strain SS14).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Phallomycetidae; Geastrales; Sphaerobolaceae; Sphaerobolus.
OX   NCBI_TaxID=990650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS14;
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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 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}.
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; KN837114; KIJ44869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9VD04; -.
DR   SMR; A0A0C9VD04; -.
DR   EnsemblFungi; KIJ44869; KIJ44869; M422DRAFT_47084.
DR   HOGENOM; CLU_042538_2_1_1; -.
DR   OrthoDB; 1143139at2759; -.
DR   Proteomes; UP000054279; 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..347
FT                   /note="Sesquiterpene synthase M422DRAFT_47084"
FT                   /id="PRO_0000451266"
FT   MOTIF           93..97
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:P0DL13"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT   BINDING         334..335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UR08"
SQ   SEQUENCE   347 AA;  39664 MW;  011F16F61EEF43C9 CRC64;
     MPLLSCSQTF RLPPLHETFS VFPDNGLNPN YNACRAQSRA WISKYNVQVC GPKMRAFMDN
     CNFELSNAYV YPYAQPAGLR ATMDLANILW LYDEYTDMQT GEDAAKAAVT VSKTLLNPEY
     DDDTWICHMM RDFYVNHIQK CRPNVAHRFI ENFCRYTEVV GTEAKLREKN EVLDIPGYVA
     LRREISAVRT CFDLVEYCLD LDFPDYVHKD PIFVIGYNAA MDLVFWANDL FSYNSEQAKG
     HAAANVVTVI MTSKKMNLQS TVDFIAGFCE ALTFQLLDAK RALSLHEDPT FSRDAVRCLE
     AFGDWVRGND AWSFATTRYF GPENKIVKET RIVKLKAPVE ESVALKE