ID   OPS6_BEAB2              Reviewed;         218 AA.
AC   J4UHQ8;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Glutathione S-transferase-like protein OpS6 {ECO:0000303|PubMed:26305932};
DE            EC=2.5.1.- {ECO:0000305|PubMed:26305932};
DE   AltName: Full=Oosporein biosynthesis protein 6 {ECO:0000303|PubMed:26305932};
GN   Name=OpS6 {ECO:0000303|PubMed:26305932}; ORFNames=BBA_08184;
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860;
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.-H., Zheng P., Wang Z.-L., Zhang S., Xie X.-Q., Shang Y.,
RA   St Leger R.J., Zhao G.-P., Wang C., Feng M.-G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RX   PubMed=26305932; DOI=10.1073/pnas.1503200112;
RA   Feng P., Shang Y., Cen K., Wang C.;
RT   "Fungal biosynthesis of the bibenzoquinone oosporein to evade insect
RT   immunity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11365-11370(2015).
CC   -!- FUNCTION: Glutathione S-transferase-like protein; part of the gene
CC       cluster that mediates the biosynthesis of the bibenzoquinone oosporein,
CC       a metabolite required for fungal virulence that acts by evading host
CC       immunity to facilitate fungal multiplication in insects
CC       (PubMed:26305932). The non-reducing polyketide synthase OpS1 produces
CC       orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units
CC       (PubMed:26305932). Orsellinic acid is then hydroxylated to benzenetriol
CC       by the hydroxylase OpS4 (PubMed:26305932). The intermediate is oxidized
CC       either nonenzymatically to 5,5'-dideoxy-oosporein or enzymatically to
CC       benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932). The latter
CC       is further dimerized to oosporein by the catalase OpS5
CC       (PubMed:26305932). OpS6 probably functions en route for protecting
CC       cells against oxidative stress by scavenging any leaked free radical
CC       form of benzenetetrol by activating the thiol group of glutathione
CC       (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:26305932}.
CC   -!- INDUCTION: Expression is positively regulated by the oosporein cluster
CC       specific regulator OpS3 that binds the promoter at a 5'-CGGA-3' motif
CC       (PubMed:26305932). Expression is negatively regulated by the global
CC       transcription factor Msn2 that binds the stress-response element 5'-
CC       AGGGG-3' (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC   -!- DISRUPTION PHENOTYPE: Does not impair the production of oosporein
CC       (PubMed:26305932). {ECO:0000269|PubMed:26305932}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; JH725181; EJP62797.1; -; Genomic_DNA.
DR   RefSeq; XP_008601503.1; XM_008603281.1.
DR   AlphaFoldDB; J4UHQ8; -.
DR   SMR; J4UHQ8; -.
DR   STRING; 655819.J4UHQ8; -.
DR   EnsemblFungi; EJP62797; EJP62797; BBA_08184.
DR   GeneID; 19891196; -.
DR   HOGENOM; CLU_011226_14_2_1; -.
DR   InParanoid; J4UHQ8; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; Transferase; Virulence.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase-like protein OpS6"
FT                   /id="PRO_0000438576"
FT   DOMAIN          5..86
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT   DOMAIN          92..218
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ   SEQUENCE   218 AA;  24380 MW;  7725C22E8BFD85A2 CRC64;
     MASLQPIKLY AHKKGPNPWK VALILEELGL PYETTYLEFP DAKVEPYISL NPNGKLPAIQ
     DPNHSIELFE SGAIIEYLIE QYDKDGKLSH ESLQDKSLAR AWLHLQMSAQ APVIGYKVWM
     GRTYDASQIV SANEFLTLEI KRVLGVLDKH LAKMGGPYLL GSKVSYADLA FVPHYMMLPL
     FVPDYDPATE YPHFAAWLAA LKERPAVKKI AATKAALA