ID GSTU1_ORYSI Reviewed; 231 AA. AC A2XMN2; O65032; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Probable glutathione S-transferase GSTU1; DE EC=2.5.1.18; GN Name=GSTU1; Synonyms=GST1; ORFNames=OsI_013325; OS Oryza sativa subsp. indica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39946; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Milyang 23; RA Yun C.-H., Lee M.C., Park J.H., Eun M.Y.; RT "Nucleotide sequence of rice glutathione S-transferase."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [3] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=15069639; DOI=10.1007/s00438-004-1006-8; RA Soranzo N., Sari Gorla M., Mizzi L., De Toma G., Frova C.; RT "Organisation and structural evolution of the rice glutathione S- RT transferase gene family."; RL Mol. Genet. Genomics 271:511-521(2004). CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of CC exogenous and endogenous hydrophobic electrophiles. 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 -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}. 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; AF050102; AAC05216.1; -; mRNA. DR EMBL; CM000128; EAY92092.1; -; Genomic_DNA. DR PIR; T02765; T02765. DR PDB; 1OYJ; X-ray; 1.95 A; A/B/C/D=1-231. DR PDBsum; 1OYJ; -. DR AlphaFoldDB; A2XMN2; -. DR SMR; A2XMN2; -. DR STRING; 39946.A2XMN2; -. DR EnsemblPlants; BGIOSGA009694-TA; BGIOSGA009694-PA; BGIOSGA009694. DR Gramene; BGIOSGA009694-TA; BGIOSGA009694-PA; BGIOSGA009694. DR HOGENOM; CLU_011226_18_2_1; -. DR OMA; YYSWFEA; -. DR Proteomes; UP000007015; Chromosome 3. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro. 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:SF732; GLUTATHIONE S-TRANSFERASE GSTU1-RELATED; 1. DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF13417; GST_N_3; 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 1: Evidence at protein level; KW 3D-structure; Reference proteome; Transferase. FT CHAIN 1..231 FT /note="Probable glutathione S-transferase GSTU1" FT /id="PRO_0000295653" FT DOMAIN 5..84 FT /note="GST N-terminal" FT DOMAIN 97..220 FT /note="GST C-terminal" FT BINDING 15 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 42 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 68..69 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT CONFLICT 88 FT /note="S -> P (in Ref. 1; AAC05216)" FT /evidence="ECO:0000305" FT CONFLICT 90 FT /note="A -> G (in Ref. 1; AAC05216)" FT /evidence="ECO:0000305" FT CONFLICT 99 FT /note="Y -> F (in Ref. 1; AAC05216)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="Q -> H (in Ref. 1; AAC05216)" FT /evidence="ECO:0000305" FT CONFLICT 175..179 FT /note="WFYSY -> CSTAT (in Ref. 1; AAC05216)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="C -> R (in Ref. 1; AAC05216)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="A -> V (in Ref. 1; AAC05216)" FT /evidence="ECO:0000305" FT STRAND 6..11 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 16..28 FT /evidence="ECO:0007829|PDB:1OYJ" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 44..49 FT /evidence="ECO:0007829|PDB:1OYJ" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:1OYJ" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:1OYJ" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 69..79 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 97..120 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 127..148 FT /evidence="ECO:0007829|PDB:1OYJ" FT STRAND 154..161 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 164..169 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 170..174 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 176..183 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 187..190 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 192..201 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 205..210 FT /evidence="ECO:0007829|PDB:1OYJ" FT HELIX 214..223 FT /evidence="ECO:0007829|PDB:1OYJ" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:1OYJ" SQ SEQUENCE 231 AA; 25832 MW; 42C953E8F540DAB0 CRC64; MAEEKELVLL DFWVSPFGQR CRIAMAEKGL EFEYREEDLG NKSDLLLRSN PVHRKIPVLL HAGRPVSESL VILQYLDDAF PGTPHLLSPA NSGDADAAYA RATARFWADY VDRKLYDCGS RLWRLKGEPQ AAAGREMAEI LRTLEAELGD REFFGGGGGG RLGFVDVALV PFTAWFYSYE RCGGFSVEEV APRLAAWARR CGRIDSVAKH LPSPEKVYDF VGVLKKKYGV E //