ID   BTPSL_METAF             Reviewed;         355 AA.
AC   A0A0B4EB91;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Sesquiterpene synthase MAN_10655 {ECO:0000303|PubMed:31239482};
DE            EC=4.2.3.- {ECO:0000269|PubMed:31239482};
DE   AltName: Full=Bacterial terpene synthase-like protein MAN_10655 {ECO:0000303|PubMed:31239482};
DE            Short=BTPSL {ECO:0000303|PubMed:31239482};
GN   ORFNames=MAN_10655;
OS   Metarhizium anisopliae (strain ARSEF 549).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=1276135;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 549;
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 9 sesquiterpenes including gamma-cadinene, delta-
CC       cadinene, alpha-cadinene, alpha-cadinol, beta-elemene, (E)-beta-
CC       caryophyllene, germacrene D, gamma-muurolene and an unidentified
CC       oxygen-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; AZNF01000028; KID59485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B4EB91; -.
DR   SMR; A0A0B4EB91; -.
DR   EnsemblFungi; KID59485; KID59485; MAN_10655.
DR   HOGENOM; CLU_042538_4_2_1; -.
DR   Proteomes; UP000031186; 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 MAN_10655"
FT                   /id="PRO_0000451052"
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;  40492 MW;  6F6AA6CFC391971F CRC64;
     MEKQRLKAQL SSLRVPLFSV PWPEQCSNKA EVVEARMMKW ADEHNLLVTD EYRNRVIRTR
     YGLLAARCYP NAGDELLQVI ADYLVWFFLI DDLFVDCVEV ATDETIRNLT AMVDVLDLNV
     SGSPPVFGEL AWLDVCQRLR RLLQVEAFER FAQGMRLWAT TAALQILNHL RPTSVSIREY
     QTIRRHTSGM NPCTSLADAA NKGSVQACEF YNADVQTLVR QTNNIVCWAN DIQSLRIEIH
     QPGQFRNMVT IYAQQGQSLQ DAVETAATRV NKEIASFCEL ANAFTARDIS HELHGFIDGL
     KYWIRGYLDW VVHDTLRYAD QFIESDADDR RFSAPDLSLL NNSCSSVTES TRSLV