BTPSL_METGA
ID BTPSL_METGA Reviewed; 348 AA.
AC A0A0B4GN88;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Sesquiterpene synthase MGU_11447 {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 MGU_11447 {ECO:0000303|PubMed:31239482};
DE Short=BTPSL {ECO:0000303|PubMed:31239482};
GN ORFNames=MGU_11447;
OS Metarhizium guizhouense (strain ARSEF 977).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1276136;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 977;
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). Produces both corvol ether A and corvol ether B in
CC similar concentrations (PubMed:31239482).
CC {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; AZNH01000187; KID81182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4GN88; -.
DR SMR; A0A0B4GN88; -.
DR EnsemblFungi; KID81182; KID81182; MGU_11447.
DR HOGENOM; CLU_042538_4_2_1; -.
DR Proteomes; UP000031192; 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..348
FT /note="Sesquiterpene synthase MGU_11447"
FT /id="PRO_0000451047"
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 348 AA; 39569 MW; 598856F753C12C7A CRC64;
MEKQRLKAQL SSLRVPLFSV PWPGQCSNKA EVIEARMMKW ADEHNLLVTD EYRNRVIRTR
YGLLAARCYP NAGEVLLQAI ADYLVWFFLA DDLFVDRVEV ATDETIRNLT AMVDVLDLNV
AGSPPVFGEL AWLDVCQRLR RLLQAETFER FAQGMRLWAT TAALQILNHL RPTSVGIREY
QTIRRHTSGM NPCASLADAA NKGSVQACEF YDADVQTLVR QTNNIVCWAN DIQSLRIEIH
QPGQFRNIVT IYAQQGQSLQ DAVETTATRV NKEIAGFCEL ADAVTARPIS DELHGLIDGL
KYWIRGYLDW VVHDTMRYAD QFIESDADDR RFSAPDLSLL KKKLLVCD
