ID A0A0D0EBP7_9AGAM Unreviewed; 183 AA.
AC A0A0D0EBP7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=PAXRUDRAFT_9844 {ECO:0000313|EMBL:KIK97990.1};
OS Paxillus rubicundulus Ve08.2h10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=930991 {ECO:0000313|EMBL:KIK97990.1, ECO:0000313|Proteomes:UP000054538};
RN [1] {ECO:0000313|EMBL:KIK97990.1, ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|EMBL:KIK97990.1,
RC ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Jargeat P., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ve08.2h10 {ECO:0000313|Proteomes:UP000054538};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000710};
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; KN824911; KIK97990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0EBP7; -.
DR STRING; 930991.A0A0D0EBP7; -.
DR HOGENOM; CLU_011226_14_0_1; -.
DR InParanoid; A0A0D0EBP7; -.
DR OrthoDB; 1328078at2759; -.
DR Proteomes; UP000054538; Unassembled WGS sequence.
DR CDD; cd03048; GST_N_Ure2p_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054538}.
FT DOMAIN 2..94
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 101..183
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 183 AA; 20701 MW; 87F363630989F53C CRC64;
MSKALLFYTA PTPNGHKVSV MLEELKAAYG SVLDYEVEKI DISTNRQKEP WFIALNPNGR
IPVIVDRTHK PDPFPVFESA AILLYLVRKY DTEGRFTFPA GSDDESVMLQ WIFFAHGGVG
PMQGQAHHFR NYAPEDIPYG KKRYTDEVGR LYNVLNIRLE GRDYLAGPGK GKLSIADINV
VPW
//
