ID C5WUJ4_SORBI Unreviewed; 244 AA. AC C5WUJ4; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 72. DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102}; DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102}; GN ORFNames=SORBI_3001G318800 {ECO:0000313|EMBL:EER94614.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER94614.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EER94614.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). RN [2] {ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=29161754; DOI=10.1111/tpj.13781; RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D., RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A., RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.; RT "The Sorghum bicolor reference genome: improved assembly, gene annotations, RT a transcriptome atlas, and signatures of genome organization."; RL Plant J. 93:338-354(2018). 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. CC {ECO:0000256|RuleBase:RU369102}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM000760; EER94614.1; -; Genomic_DNA. DR RefSeq; XP_002467616.1; XM_002467571.1. DR AlphaFoldDB; C5WUJ4; -. DR STRING; 4558.C5WUJ4; -. DR EnsemblPlants; EER94614; EER94614; SORBI_3001G318800. DR GeneID; 8062885; -. DR Gramene; EER94614; EER94614; SORBI_3001G318800. DR KEGG; sbi:8062885; -. DR eggNOG; KOG0406; Eukaryota. DR HOGENOM; CLU_011226_18_0_1; -. DR InParanoid; C5WUJ4; -. DR OMA; CICESQI; -. DR OrthoDB; 397381at2759; -. DR Proteomes; UP000000768; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central. DR GO; GO:0042221; P:response to chemical; 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; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1. DR PANTHER; PTHR11260:SF476; GLUTATHIONE TRANSFERASE; 1. DR Pfam; PF13410; GST_C_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000000768}; KW Transferase {ECO:0000256|RuleBase:RU369102}. FT DOMAIN 9..88 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 96..234 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 244 AA; 26434 MW; 0A1470ABD1C531EA CRC64; MAGAGEGGDE LKLLGNLTSP FVLRVKLALS FKGLSYEYIA EDLQNKSNLL LSSNPVHKKV PVLIHKGEPI CESQVIVQYI DEAFQGTDGP SLLPADPYER AVARFWAAYV FDKLLPAWLQ SFMGKTDEEK AEGLKQTFAA VDQLEAAFKE CSKGKPFFGG DSVGHMDVAL GSLVPWGVYA GEKLYGFRLF DAARSPLLNA WLERFAALDA AKAVLPDADR LVDYAKMKRA EAEAAAAAAA SSNN //