BTPS1_METBS
ID BTPS1_METBS Reviewed; 332 AA.
AC A0A0B4FWC3;
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 MBR_10393 {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 MBR_10393 {ECO:0000303|PubMed:31239482};
DE Short=BTPSL {ECO:0000303|PubMed:31239482};
GN ORFNames=MBR_10393;
OS Metarhizium brunneum (strain ARSEF 3297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1276141;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 3297;
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 B
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; AZNG01000036; KID60519.1; -; Genomic_DNA.
DR RefSeq; XP_014539580.1; XM_014684094.1.
DR AlphaFoldDB; A0A0B4FWC3; -.
DR SMR; A0A0B4FWC3; -.
DR EnsemblFungi; KID60519; KID60519; MBR_10393.
DR GeneID; 26247663; -.
DR HOGENOM; CLU_042538_4_2_1; -.
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..332
FT /note="Sesquiterpene synthase MBR_10393"
FT /id="PRO_0000451048"
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 332 AA; 37835 MW; 4F7D7AC8BE2580DF CRC64;
MEKQRLTAQL SSLRVPLFSV PWPGQCSNKA EVIEARMMKW ADEHNLLVTD EYRNRVIRTR
YGLLAARCYP NAGEELLQAI ADCLVWFFLA DDLFVDRVEV ATDETIRNLT AMVDVLDLNV
AGSPPVFGEL AWLDVCQRLR RLLQAEAFER FAQGMRLWAT TAALQILNHL RPTSVGMREY
QTIRRHTSGM NPCTSLADAA NKGSVQACEF YDADVQTLVR QTNNIVCWAN DIQSLRIEIH
QPGQFRNMVT IYAQQGQSLQ DAVETTATRV NKEIASFCEL ADAVTARPIS DELHGLIDGL
KYWIRGYLDW VVHDTLRYAD QFIESDADDR RF
