PROS_DENBC
ID PROS_DENBC Reviewed; 353 AA.
AC A0A4S8MAF3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Delta(6)-protoilludene synthase K435DRAFT_659367 {ECO:0000303|PubMed:32233445};
DE EC=4.2.3.135 {ECO:0000269|PubMed:32233445};
DE AltName: Full=Sesquiterpene synthase K435DRAFT_659367 {ECO:0000303|PubMed:32233445};
DE AltName: Full=Terpene cyclase K435DRAFT_659367 {ECO:0000303|PubMed:32233445};
GN ORFNames=K435DRAFT_659367;
OS Dendrothele bispora (strain CBS 962.96).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricales incertae sedis; Dendrothele.
OX NCBI_TaxID=1314807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 962.96;
RX PubMed=30886374; DOI=10.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foeldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szoellosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Daemon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvoelgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
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 delta(6)-protoilludene.
CC {ECO:0000269|PubMed:32233445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = Delta(6)-protoilludene +
CC diphosphate; Xref=Rhea:RHEA:34695, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:68655, ChEBI:CHEBI:175763; EC=4.2.3.135;
CC Evidence={ECO:0000269|PubMed:32233445};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34696;
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. {ECO:0000305}.
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DR EMBL; ML179122; THU99250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4S8MAF3; -.
DR SMR; A0A4S8MAF3; -.
DR Proteomes; UP000297245; 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..353
FT /note="Delta(6)-protoilludene synthase K435DRAFT_659367"
FT /id="PRO_0000451269"
FT MOTIF 97..101
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P0DL13"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 94
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 353 AA; 40908 MW; 63BECCDAE846B105 CRC64;
MTVPIPTSTE QSSAPTRFFI PDTLANWPWP RALNPAYEQC KADSAAWCEK YKAFSPKAQK
AFNLCDFNLL ASLAYAHLPE DVNRVGCDLM NLFFVVDEHS DAMDKNSVHV WVEIIMDALR
NPTKPRPDDE PIVGEISRTF WENAIKCLGP TSQKRFIETF ETYLYAVIVQ ADDRDHHVFR
DVDSYMVVRR DTIGAKPSFA LLEHNMDLPD DVFNHPLLED LRTWCIDMLI LGNDLCSYNV
EQSRGDDGHN IVKLVMLQEN IDLHGAMQYI SDMHDDLADK FLRNYKNMPS WGQPIDEWVT
RYIEGLGNWV RANDAWSFES WRYFKYDGLR IQKERWVELL PPANKEDLTS SSE
