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Database: UniProt
Entry: H0EYA0_GLAL7
LinkDB: H0EYA0_GLAL7
Original site: H0EYA0_GLAL7 
ID   H0EYA0_GLAL7            Unreviewed;       252 AA.
AC   H0EYA0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   ORFNames=M7I_7799 {ECO:0000313|EMBL:EHK96470.1};
OS   Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK96470.1, ECO:0000313|Proteomes:UP000005446};
RN   [1] {ECO:0000313|EMBL:EHK96470.1, ECO:0000313|Proteomes:UP000005446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX   PubMed=22302591; DOI=10.1128/EC.05302-11;
RA   Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT   "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT   of a species from the Helotiaceae family.";
RL   Eukaryot. Cell 11:250-250(2012).
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, ECO:0000256|RuleBase:RU003494}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK96470.1}.
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DR   EMBL; AGUE01000248; EHK96470.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0EYA0; -.
DR   HOGENOM; CLU_011226_14_0_1; -.
DR   InParanoid; H0EYA0; -.
DR   Proteomes; UP000005446; Unassembled WGS sequence.
DR   CDD; cd10291; GST_C_YfcG_like; 1.
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; IPR004046; GST_C.
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; PF00043; GST_C; 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:UP000005446}.
FT   DOMAIN          4..90
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          97..233
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   252 AA;  28587 MW;  551CBD8D29E674D1 CRC64;
     MARTPDIHLY TTQTPNGIKI SITLEELGLP YKVTKIDITK DTQKEPWFLA INPNGRIPAL
     TDTFKDGKQI NLFESGGIQQ YLVDEYDTDY KISYPKGTRE YYEMINWLFF LNAGVGPMQG
     QANHFSRYAP EHIEYGVKRY TNETRRLYGV LNTHLEKSTS GYLVGDKCTI ADIAHWGWVA
     SAGWAGVEIN EFPALKKWEE QMAARPALEK GRHVPSPHTI KETLKDPEKM KAIAESSKAW
     IQSGMAADAK KK
//
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