ID   B9WFZ4_CANDC            Unreviewed;       219 AA.
AC   B9WFZ4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   OrderedLocusNames=Cd36_42860 {ECO:0000313|CGD:CAL0000160964};
GN   ORFNames=CD36_42860 {ECO:0000313|EMBL:CAX42163.1};
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX42163.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX42163.1, ECO:0000313|Proteomes:UP000002605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC   {ECO:0000313|Proteomes:UP000002605};
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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}.
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DR   EMBL; FM992691; CAX42163.1; -; Genomic_DNA.
DR   RefSeq; XP_002419948.1; XM_002419903.1.
DR   AlphaFoldDB; B9WFZ4; -.
DR   GeneID; 8047693; -.
DR   KEGG; cdu:CD36_42860; -.
DR   CGD; CAL0000160964; Cd36_42860.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_14_0_1; -.
DR   OrthoDB; 1404190at2759; -.
DR   Proteomes; UP000002605; Chromosome 4.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   Transferase {ECO:0000313|EMBL:CAX42163.1}.
FT   DOMAIN          2..88
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          95..219
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   219 AA;  25111 MW;  3801AF4D9D5B07AD CRC64;
     MVKPIQLYTF ATPNGFKASI FLEILGLAYE TTVVDITKNE SKSDWFVKLN PNGRIPTIVD
     PNFKDGEITI SQTGAILQYL ADNYDKEHKY SYPFGTENYY KTLEYLIFQV SENGPIQGQL
     NHFKLFAKEK IEYGITRYEN DTKRIYGVYE DILSRNSAND SKYLVGDRYT VADFALFGWA
     YCLPKVGIDI HDWPLLGKWF DTLNANPAVI KGVNVPEKK
//