PROS_HETIT
ID PROS_HETIT Reviewed; 345 AA.
AC W4JX79;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Delta(6)-protoilludene synthase HETIRDRAFT_454193 {ECO:0000303|PubMed:32233445};
DE EC=4.2.3.135 {ECO:0000269|PubMed:32233445};
DE AltName: Full=Sesquiterpene synthase HETIRDRAFT_454193 {ECO:0000303|PubMed:32233445};
DE AltName: Full=Terpene cyclase HETIRDRAFT_454193 {ECO:0000303|PubMed:32233445};
GN ORFNames=HETIRDRAFT_454193;
OS Heterobasidion irregulare (strain TC 32-1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Bondarzewiaceae; Heterobasidion;
OC Heterobasidion annosum species complex.
OX NCBI_TaxID=747525;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC 32-1;
RX PubMed=22463738; DOI=10.1111/j.1469-8137.2012.04128.x;
RA Olson A., Aerts A., Asiegbu F., Belbahri L., Bouzid O., Broberg A.,
RA Canback B., Coutinho P.M., Cullen D., Dalman K., Deflorio G.,
RA van Diepen L.T., Dunand C., Duplessis S., Durling M., Gonthier P.,
RA Grimwood J., Fossdal C.G., Hansson D., Henrissat B., Hietala A.,
RA Himmelstrand K., Hoffmeister D., Hogberg N., James T.Y., Karlsson M.,
RA Kohler A., Kues U., Lee Y.H., Lin Y.C., Lind M., Lindquist E., Lombard V.,
RA Lucas S., Lunden K., Morin E., Murat C., Park J., Raffaello T., Rouze P.,
RA Salamov A., Schmutz J., Solheim H., Stahlberg J., Velez H., de Vries R.P.,
RA Wiebenga A., Woodward S., Yakovlev I., Garbelotto M., Martin F.,
RA Grigoriev I.V., Stenlid J.;
RT "Insight into trade-off between wood decay and parasitism from the genome
RT of a fungal forest pathogen.";
RL New Phytol. 194:1001-1013(2012).
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; KI925462; ETW78167.1; -; Genomic_DNA.
DR RefSeq; XP_009550163.1; XM_009551868.1.
DR AlphaFoldDB; W4JX79; -.
DR SMR; W4JX79; -.
DR EnsemblFungi; ETW78167; ETW78167; HETIRDRAFT_454193.
DR GeneID; 20676477; -.
DR KEGG; hir:HETIRDRAFT_454193; -.
DR eggNOG; ENOG502SJ0F; Eukaryota.
DR HOGENOM; CLU_042538_5_0_1; -.
DR OrthoDB; 1143139at2759; -.
DR Proteomes; UP000030671; 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; IPR001005; SANT/Myb.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..345
FT /note="Delta(6)-protoilludene synthase HETIRDRAFT_454193"
FT /id="PRO_0000451270"
FT DOMAIN 277..327
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT MOTIF 84..88
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:P0DL13"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 325..326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UR08"
FT SITE 81
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 345 AA; 39668 MW; 4371EFFBE500A6DC CRC64;
MAQKIYIPDT LANWKWPPHL NPHYPEVKRE SAAWLASFGA FSPKAQDAFD RCDFNLLASF
AYPLAKKEHL RSGCDLMNLF FVIDEYSDVA EADEVQRQAD IVMDALRNPH KPRPKGEWVG
GEVTRQFWEL AIKTASPQSQ KRFIATFDTY TQSVVQQAAD RTHSYIRDIK SYFEVRRNTI
GAKPSFALLE LEMDLPDKVI EHPIIQDLSI LTIDMLHLGN DIASYNLEQA RGDDSHNIVT
IAMNQLKTDV AGAMKWVDNH HKELERKFNE SFEKLPKWGE PIDSQVARYV DGLGNWVRAN
DQWSFVSERY FGKKGPEIMK SRWVTLLPKE RTEDIGPQVV DDSLL
