BTPSL_METRA
ID BTPSL_METRA Reviewed; 355 AA.
AC E9F8R9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Sesquiterpene synthase MAA_08668 {ECO:0000303|PubMed:31239482};
DE EC=4.2.3.- {ECO:0000269|PubMed:31239482};
DE AltName: Full=Bacterial terpene synthase-like protein MAA_08668 {ECO:0000303|PubMed:31239482};
DE Short=BTPSL {ECO:0000303|PubMed:31239482};
GN ORFNames=MAA_08668;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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 [3]
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 9 sesquiterpenes including gamma-cadinene, delta-
CC cadinene, alpha-cadinene, alpha-cadinol, beta-elemene, (E)-beta-
CC caryophyllene, germacrene D, nerolidol and an unidentified oxygen-
CC containing sesquiterpene (PubMed:31239482).
CC {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; ADNJ02000004; EFY95860.1; -; Genomic_DNA.
DR RefSeq; XP_007824857.1; XM_007826666.1.
DR AlphaFoldDB; E9F8R9; -.
DR SMR; E9F8R9; -.
DR EnsemblFungi; EFY95860; EFY95860; MAA_08668.
DR GeneID; 19262954; -.
DR KEGG; maj:MAA_08668; -.
DR HOGENOM; CLU_042538_4_2_1; -.
DR Proteomes; UP000002498; 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 MAA_08668"
FT /id="PRO_0000451051"
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; 40136 MW; 184426CB9738271A CRC64;
MEKQRLKAQL SSLRVPLFSV PWPGQCSNKA EVVEARMMKW ADEHNLLVTD EYRNRVIRTR
YGLLAARCYP NAGEELLQVI ADYLVWFFLT DDLFVDRVEV ATDETIRNLT AMVDVLDLNV
AGSPPVFGEL AWLDVCQRLR RLLQVEAFER FAQGMRLWAT TAALQILNHL RPTSVGIQEY
QTIRRHTSGM NPCTSLADAA NKGSVQACEF YDADVQTLVR QTNNIVSWAN DIQSLRREIH
QPGQFRNMVT ICAQQGQSIQ DSVETTATRV NKEIAGFCGL ADAVTARPIS DELHGLIDGL
KYWIRGYLDW VAHDTMRYAD HFIESDADDR RFSAPDLSLL NKSCSSVTES TSSLV
