BTPSL_METAQ
ID BTPSL_METAQ Reviewed; 349 AA.
AC E9E766;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Sesquiterpene synthase MAC_05714 {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 MAC_05714 {ECO:0000303|PubMed:31239482};
DE Short=BTPSL {ECO:0000303|PubMed:31239482};
GN ORFNames=MAC_05714;
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102;
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 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; GL698514; EFY88241.1; -; Genomic_DNA.
DR RefSeq; XP_007812054.1; XM_007813863.1.
DR AlphaFoldDB; E9E766; -.
DR SMR; E9E766; -.
DR EnsemblFungi; EFY88241; EFY88241; MAC_05714.
DR GeneID; 19250025; -.
DR KEGG; maw:MAC_05714; -.
DR eggNOG; ENOG502RKSS; Eukaryota.
DR HOGENOM; CLU_042538_4_2_1; -.
DR InParanoid; E9E766; -.
DR OMA; DLIEYAM; -.
DR OrthoDB; 1143139at2759; -.
DR Proteomes; UP000002499; 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; Reference proteome.
FT CHAIN 1..349
FT /note="Sesquiterpene synthase MAC_05714"
FT /id="PRO_0000451050"
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 349 AA; 39947 MW; 08EEDA1CAB36CF2D CRC64;
MEKQHLKSQI AALRVPTFNI AWPERRSPKA DVVEERMMKW ADHHKLLVNG EYRDRVIRTR
YGLLAARCYP NAGEELLQAI ADYFVWFFLA DDLFVDRVEV VTDETIRNLT AMIDVLDRNV
AREEPVFGEL AWLDVCQRLR DLLQPEAFQR FAQGMRLWAT TAALQILNHQ RPKSVGIREY
EAIRRHTSGL NPCTSLADAA NKGSVQAHEF YQPDVQKLVL QTNNIVCWAN DIQSLGMEIQ
QPGQFRNMVT IYIQQGQSLS EAVSTTTARV NNELSDFCKL ADIVTAPSIS DELRVYVDGL
KYWIRGYMDW VVHDTERYAD KFIASDADDR CVSTLNPSLL NRSSSSATE
