ID   GST_COCIM               Reviewed;         231 AA.
AC   D2YW48; J3KIY1; J3KJ57;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable glutathione S-transferase;
DE            EC=2.5.1.18;
GN   ORFNames=CIMG_01314;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RC   STRAIN=RS;
RG   Seattle structural genomics center for infectious disease (SSGCID);
RT   "Crystal structure of putative glutathione transferase from Coccidioides
RT   immitis bound to glutathione.";
RL   Submitted (JUN-2010) to the PDB data bank.
CC   -!- FUNCTION: Probable glutathione S-transferase.
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   -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.3}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR   EMBL; GG704911; EAS35960.3; -; Genomic_DNA.
DR   RefSeq; XP_001247543.1; XM_001247542.2.
DR   PDB; 3LG6; X-ray; 2.20 A; A/B/C/D=1-231.
DR   PDB; 3N5O; X-ray; 1.85 A; A/B=1-231.
DR   PDBsum; 3LG6; -.
DR   PDBsum; 3N5O; -.
DR   AlphaFoldDB; D2YW48; -.
DR   SMR; D2YW48; -.
DR   STRING; 246410.D2YW48; -.
DR   EnsemblFungi; EAS35960; EAS35960; CIMG_01314.
DR   GeneID; 4567107; -.
DR   KEGG; cim:CIMG_01314; -.
DR   VEuPathDB; FungiDB:CIMG_01314; -.
DR   InParanoid; D2YW48; -.
DR   OMA; VYNAHRF; -.
DR   OrthoDB; 1283865at2759; -.
DR   EvolutionaryTrace; D2YW48; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd03191; GST_C_Zeta; 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; IPR005955; GST_Zeta.
DR   InterPro; IPR034330; GST_Zeta_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01262; maiA; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Transferase.
FT   CHAIN           1..231
FT                   /note="Probable glutathione S-transferase"
FT                   /id="PRO_0000404254"
FT   DOMAIN          4..96
FT                   /note="GST N-terminal"
FT   DOMAIN          105..227
FT                   /note="GST C-terminal"
FT   BINDING         14
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|Ref.3"
FT   BINDING         43
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|Ref.3"
FT   BINDING         57
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|Ref.3"
FT   BINDING         80..81
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT   BINDING         124
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|Ref.3"
FT   BINDING         128..130
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT   STRAND          5..10
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:3LG6"
FT   STRAND          59..65
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           81..91
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           106..122
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           129..137
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           142..164
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   STRAND          165..171
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           176..190
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           199..209
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           212..216
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:3N5O"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:3N5O"
SQ   SEQUENCE   231 AA;  25585 MW;  6D6D57E813D63A07 CRC64;
     MTTPNFELYG YFRSSCSGRL RIAFHLKSIP YTRHPVNLLK GEQHSDTYKS LNPTNTVPLL
     VVSNINNTVS PSSASFSIGQ SLAALEYLEE ALPTNARPLL PPISNPVARA HVRTICNIIA
     CDVQPVTNLK IQKKVKALDG DPTVWSRDLA TQGFGAVEKL LELSAGRFCV GDEITLADVC
     LVPAVWAAER VGMDLARFPI TKRVFEEMLK EEAVQKAHWQ KQEDTPEDLR A