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Database: UniProt
Entry: A0A1Q5TJF9_9EURO
LinkDB: A0A1Q5TJF9_9EURO
Original site: A0A1Q5TJF9_9EURO 
ID   A0A1Q5TJF9_9EURO        Unreviewed;       220 AA.
AC   A0A1Q5TJF9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=PENSUB_7812 {ECO:0000313|EMBL:OKP00355.1};
OS   Penicillium subrubescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP00355.1, ECO:0000313|Proteomes:UP000186955};
RN   [1] {ECO:0000313|EMBL:OKP00355.1, ECO:0000313|Proteomes:UP000186955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP00355.1,
RC   ECO:0000313|Proteomes:UP000186955};
RA   De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA   Grigoriev I., Riley R., Granchi Z.;
RT   "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL   Submitted (OCT-2016) 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|PIRNR:PIRNR006386};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC       {ECO:0000256|PIRNR:PIRNR006386}.
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:OKP00355.1}.
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DR   EMBL; MNBE01000647; OKP00355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5TJF9; -.
DR   STRING; 1316194.A0A1Q5TJF9; -.
DR   OrthoDB; 4159077at2759; -.
DR   Proteomes; UP000186955; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR014440; HCCAis_GSTk.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42943; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR42943:SF2; GLUTATHIONE S-TRANSFERASE KAPPA 1; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW   Transferase {ECO:0000256|PIRNR:PIRNR006386, ECO:0000313|EMBL:OKP00355.1}.
FT   DOMAIN          6..205
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ   SEQUENCE   220 AA;  24489 MW;  58F209FA4EE39972 CRC64;
     MAPPKITLYF DIISPFAYIA FHVLRNSPTF AKCEINYVPI LLGGLINLCD NKAPISIKNK
     DKWINVERAR WAKYFSVPIC DSPPEGFPVR TLAVQRALCV VSQKTPTKLP SVIEALYHSF
     WVQSNSKIGE PAVFAQVIES VLGQEDTKEV LSAMTQPEMK ALLTSNTDHA FKIGAFGIPW
     FECTNTAGQT EGFWGIDHLG QVVDFLGLDR SRDPGFRALL
//
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