TERS_PILCF
ID TERS_PILCF Reviewed; 345 AA.
AC A0A0C3FBR2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Sesquiterpene synthase PILCRDRAFT_825684 {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 PILCRDRAFT_825684 {ECO:0000303|PubMed:32233445};
GN ORFNames=PILCRDRAFT_825684;
OS Piloderma croceum (strain F 1598).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Piloderma.
OX NCBI_TaxID=765440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F 1598;
RG DOE Joint Genome Institute;
RA Kuo A., Tarkka M., Buscot F., Kohler A., Nagy L.G., Floudas D.,
RA Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F 1598;
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 (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 various sesquiterpenes, including beta-elemene,
CC viridiflorene and gamma-cadinene (PubMed:32233445). Gamma-cadinene is
CC the major product of PILCRDRAFT_825684 (PubMed:32233445).
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; KN833028; KIM77136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3FBR2; -.
DR SMR; A0A0C3FBR2; -.
DR EnsemblFungi; KIM77136; KIM77136; PILCRDRAFT_825684.
DR HOGENOM; CLU_042538_2_1_1; -.
DR OrthoDB; 1143139at2759; -.
DR Proteomes; UP000054166; 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 PILCRDRAFT_825684"
FT /id="PRO_0000451267"
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; 39099 MW; D463AC5A894C2048 CRC64;
MPSQSLTIRL PKFEETFSVF PDNGLNPHYA NSRAESRAWI NQYHHAVCGP NMRTFMDKCN
FELAGALFYP YANEAGLRAT MDLVNLLWLY DELTDTKTET EAVNAAHIVA CALREPDFDD
GTWICSMIKD FNQRHISKAG PNTAYRFIYN FCNYVEAVGT EAGLRAKNEI LDITTYISFR
RETSALRLTF DLVQYCLGID LPQYVHDDPV FASGYNAAMD LVCWTNDLFS YNREQAKGHA
GANVVTVIMK SKGVDIQSAV DFVGGYCEAL TSQLVEARRI LLSRSHRVYS KDAVRILEAF
GDFVRGNDQW SFASERYFGQ KNKVVKESRI VEIITPFSDL IAINE
