BTPSL_METMF
ID BTPSL_METMF Reviewed; 355 AA.
AC A0A0B4IF96;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Sesquiterpene synthase MAJ_08936 {ECO:0000303|PubMed:31239482};
DE EC=4.2.3.163 {ECO:0000269|PubMed:31239482};
DE EC=4.2.3.171 {ECO:0000269|PubMed:31239482};
DE AltName: Full=Bacterial terpene synthase-like protein MAJ_08936 {ECO:0000303|PubMed:31239482};
DE Short=BTPSL {ECO:0000303|PubMed:31239482};
GN ORFNames=MAJ_08936;
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31239482; DOI=10.1038/s41598-019-45532-1;
RA Jia Q., Chen X., Koellner T.G., Rinkel J., Fu J., Labbe J., Xiong W.,
RA Dickschat J.S., Gershenzon J., Chen F.;
RT "Terpene synthase genes originated from bacteria through horizontal gene
RT transfer contribute to terpenoid diversity in fungi.";
RL Sci. Rep. 9:9223-9223(2019).
CC -!- FUNCTION: Terpene synthase that catalyzes the conversion of (2E,6E)-
CC farnesyl diphosphate (FPP) into sesquiterpenes which are important for
CC fungi-environment interactions (PubMed:31239482). Produces a mixture
CC consisting of 8 sesquiterpenes including corvol ethers A and B, as well
CC as traces of epizonarene, gamma-cadinene, delta-cadinene, alpha-
CC cadinene, alpha-cadinol, and an unidentified sesquiterpene
CC (PubMed:31239482). The major product is corvol ether A
CC (PubMed:31239482). {ECO:0000269|PubMed:31239482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-corvol ether B +
CC diphosphate; Xref=Rhea:RHEA:53644, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:137536, ChEBI:CHEBI:175763;
CC EC=4.2.3.163; Evidence={ECO:0000269|PubMed:31239482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53645;
CC Evidence={ECO:0000269|PubMed:31239482};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (+)-corvol ether A +
CC diphosphate; Xref=Rhea:RHEA:53648, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:137535, ChEBI:CHEBI:175763;
CC EC=4.2.3.171; Evidence={ECO:0000269|PubMed:31239482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53649;
CC Evidence={ECO:0000269|PubMed:31239482};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B5HDJ6};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:B5HDJ6};
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Xaa-Asp (DDXXXD) motif is important for the
CC catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250|UniProtKB:B5HDJ6}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AZNE01000088; KID95099.1; -; Genomic_DNA.
DR RefSeq; XP_014574093.1; XM_014718607.1.
DR AlphaFoldDB; A0A0B4IF96; -.
DR SMR; A0A0B4IF96; -.
DR EnsemblFungi; KID95099; KID95099; MAJ_08936.
DR HOGENOM; CLU_042538_4_2_1; -.
DR OrthoDB; 1143139at2759; -.
DR Proteomes; UP000031176; 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.
FT CHAIN 1..355
FT /note="Sesquiterpene synthase MAJ_08936"
FT /id="PRO_0000451046"
FT MOTIF 91..96
FT /note="DDXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 88
FT /note="Plays a critical role in the stabilization of
FT intermediate cation"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
FT SITE 92
FT /note="Plays a critical role for substrate recognition"
FT /evidence="ECO:0000250|UniProtKB:B5HDJ6"
SQ SEQUENCE 355 AA; 40204 MW; A504A4995DA9DBE2 CRC64;
MEKQRLKAQL SSLRVPLFSV PWPGQCSNKA EVIEARMMKW ADEHNLLVTD EYRNRVIRTR
YGLLAARCYP NAGEVLLQAI ADYLVWFFLA DDLFVDRVEV ATDETIRNLT AMVDVLDLNV
AGSPPVFGEL AWLDVCQRLR RLLQAEAFER FAQGMRLWAT TAALQILNHL RPTPVGIREY
QTIRRHTSGL NPCTSLADAA NKGSVQACEF YDADVQTLVR QTNNIVCWAN DIQSLRIEIH
QPGQFRNMVT IYAQQGQSLQ DAVETTATRV NKEIAGFCEL ADAVTARPIS DELHGLIDGL
EYWIRGYLDW VVHDTMRYAD QFIESDADDR RFSAPDLSLL KKNCSSVTES TSSLV
