ID A0A0D2ES19_9EURO Unreviewed; 222 AA.
AC A0A0D2ES19;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=Z517_09473 {ECO:0000313|EMBL:KIW77027.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW77027.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW77027.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW77027.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
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|RuleBase:RU003494}.
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DR EMBL; KN846974; KIW77027.1; -; Genomic_DNA.
DR RefSeq; XP_013280835.1; XM_013425381.1.
DR AlphaFoldDB; A0A0D2ES19; -.
DR STRING; 1442368.A0A0D2ES19; -.
DR GeneID; 25308963; -.
DR VEuPathDB; FungiDB:Z517_09473; -.
DR HOGENOM; CLU_011226_5_1_1; -.
DR OrthoDB; 639740at2759; -.
DR Proteomes; UP000053029; Unassembled WGS sequence.
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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43900:SF98; GLUTATHIONE S-TRANSFERASE 2; 1.
DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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:UP000053029}.
FT DOMAIN 2..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 91..220
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 222 AA; 25014 MW; 1D05073BA8DF9D97 CRC64;
MPAFTLYGAR GSTNTDRVRL TLAEGGFTDY DFVLANLQKG EQKTEENMKR HPWGKIPVVV
FPSGFTLYES RAICKYLTRK YSFPLLPSAS DIEATALFDQ AESAEILYFA EPAGKIAFEK
FAKRFMGLSP DETVVSDALR SVEMFFDVAD RLLRDREYVA GNAFTLADIY YIPLVQRLFA
CGYGDVIFGR EAVSAWWKRC MDRPAIQKMV AADREAMSNA GK
//
