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Database: UniProt
Entry: A0A0D2QYG6_GOSRA
LinkDB: A0A0D2QYG6_GOSRA
Original site: A0A0D2QYG6_GOSRA 
ID   A0A0D2QYG6_GOSRA        Unreviewed;       240 AA.
AC   A0A0D2QYG6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN   ORFNames=B456_004G032100 {ECO:0000313|EMBL:KJB22156.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB22156.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB22156.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
CC   -!- FUNCTION: Is involved in the conjugation of reduced glutathione to a
CC       wide number of exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000256|RuleBase:RU369102}.
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         ECO:0000256|RuleBase:RU369102};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|RuleBase:RU369102}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Tau family.
CC       {ECO:0000256|ARBA:ARBA00025743}.
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DR   EMBL; CM001743; KJB22156.1; -; Genomic_DNA.
DR   RefSeq; XP_012473190.1; XM_012617736.1.
DR   AlphaFoldDB; A0A0D2QYG6; -.
DR   STRING; 29730.A0A0D2QYG6; -.
DR   EnsemblPlants; KJB22156; KJB22156; B456_004G032100.
DR   GeneID; 105790239; -.
DR   Gramene; KJB22156; KJB22156; B456_004G032100.
DR   KEGG; gra:105790239; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   OMA; VWYSPYA; -.
DR   OrthoDB; 924401at2759; -.
DR   Proteomes; UP000032304; Chromosome 4.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0009407; P:toxin catabolic process; IEA:UniProt.
DR   CDD; cd03185; GST_C_Tau; 1.
DR   CDD; cd03058; GST_N_Tau; 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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF673; GLUTATHIONE S-TRANSFERASE U7; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-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   Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW   Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW   Transferase {ECO:0000256|RuleBase:RU369102}.
FT   DOMAIN          4..84
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..222
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   240 AA;  26755 MW;  33F62B470F44D9A1 CRC64;
     MGKSEVKLLG AWPSPFMLRV RIALHLKSIN YEFIEVDLLG PKSELVLKSN PIYKKIPVLF
     HDGNTILESQ IIVQYIDEVW HNAPSILPSD AAQRADSRFW VAYFDDKLVP ALIVALAAKS
     KDKKNAAIAE LEQGLVHLEE AASTKLSKGK ALFGGENLGY MDIALGPFLV WIGIIEKLNG
     VKLLNETNTP SLLRWADSFF SHAVVKTIFP EAEKLIEFAM KLIPVLRARP ELRLLLGISD
//
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