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Database: UniProt
Entry: A0A0M8PCP2_9EURO
LinkDB: A0A0M8PCP2_9EURO
Original site: A0A0M8PCP2_9EURO 
ID   A0A0M8PCP2_9EURO        Unreviewed;       209 AA.
AC   A0A0M8PCP2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   ORFNames=ACN38_g806 {ECO:0000313|EMBL:KOS48217.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS48217.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS48217.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS48217.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-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, 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:KOS48217.1}.
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DR   EMBL; LHQQ01000007; KOS48217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8PCP2; -.
DR   STRING; 229535.A0A0M8PCP2; -.
DR   OrthoDB; 5792at2759; -.
DR   Proteomes; UP000037696; Unassembled WGS sequence.
DR   CDD; cd03057; GST_N_Beta; 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; IPR040079; Glutathione_S-Trfase.
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; 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:UP000037696}.
FT   DOMAIN          1..79
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          85..209
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   209 AA;  23177 MW;  4AF99E70F229E7A7 CRC64;
     MSEIKLFYMK GACSLLPHIL LHEAGLPFTT SAETNGSISD ELLRLNPKGK VPLLIANGEI
     ITENIAIMTY ISNQVPEKNL LGAAGTMDPI RVYEWFSWLG SAVHAVGFAA FFRPQRFTVS
     EDADVHVGIK EQAKKALLAS FKIVEDRLDG VHAVGNKFTA ADVYLLVFWR WAQSTFGLDL
     KAEFPKYCAL TETVVKRESV VKAMREEGL
//
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