ID B2BXJ1_ARALL Unreviewed; 215 AA. AC B2BXJ1; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, 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 Name=GSTU4 {ECO:0000313|EMBL:ABW81028.1}; GN ORFNames=ARALYDRAFT_320713 {ECO:0000313|EMBL:EFH57308.1}; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=81972 {ECO:0000313|EMBL:ABW81028.1}; RN [1] {ECO:0000313|EMBL:ABW81028.1} RP NUCLEOTIDE SEQUENCE. RA Schmid K.J., Navarro-Quezada A.; RT "Evolution of a short chain dehydrogenase (tropinone-reductase-like) gene RT family in the Brassicaceae."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EFH57308.1} RP NUCLEOTIDE SEQUENCE. RG US DOE Joint Genome Institute (JGI-PGF); RA Ottilar R., Schmutz J., Salamov A., Cheng J.F., Lucas S., Pitluck S., RA Gundlach H., Guo Y., Haberer G., Nasrallah J., Mayer K.F.X., RA van de Peer Y., Weigel D., Grigoriev I.V.; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EFH57308.1} RP NUCLEOTIDE SEQUENCE. RG US DOE Joint Genome Institute (JGI-PGF); RA Bakker E., Bergelson J., Cheng J.Fang., Clark R.M., Fawcett J., Gaut B., RA Grigoriev I., Gundlach H., Guo Y., Haberer G., Hollister J., Hu T.T., RA Mayer K.F.X., Nasrallah J., Nordborg M., Otillar R., Pattyn P., Schmutz J., RA Spannagl M., van de Peer Y., Wang X., Weigel D., Yang L.; RT "The basis of rapid genome size change in Arabidopsis."; RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K., RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J., RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y., RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size RT change."; RL Nat. Genet. 43:476-481(2011). 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. CC {ECO:0000256|ARBA:ARBA00025743}. 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; EU162608; ABW81028.1; -; Genomic_DNA. DR EMBL; GL348716; EFH57308.1; -; Genomic_DNA. DR RefSeq; XP_002881049.1; XM_002881003.1. DR AlphaFoldDB; B2BXJ1; -. DR STRING; 81972.B2BXJ1; -. DR EnsemblPlants; fgenesh1_pm.C_scaffold_4000770; fgenesh1_pm.C_scaffold_4000770; fgenesh1_pm.C_scaffold_4000770. DR Gramene; fgenesh1_pm.C_scaffold_4000770; fgenesh1_pm.C_scaffold_4000770; fgenesh1_pm.C_scaffold_4000770. DR eggNOG; KOG0406; Eukaryota. DR HOGENOM; CLU_011226_18_2_1; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro. 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 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; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR045074; GST_C_Tau. DR InterPro; IPR045073; Omega/Tau-like. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11260:SF533; GLUTATHIONE S-TRANSFERASE U5-RELATED; 1. DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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|ARBA:ARBA00022490}; KW Detoxification {ECO:0000256|ARBA:ARBA00022575}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}; KW Transferase {ECO:0000313|EMBL:ABW81028.1}. FT DOMAIN 1..78 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 83..207 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 215 AA; 25049 MW; 72F7F231435274D4 CRC64; MSENNELTNF VELRPFPALK LKGINYDYVE EKFESKSSLL LALNPIHKKV PVLVHNGKTI LESHVILEYI DETWPHNPIL PQDPYKRSKA RFFAKLVDEH ITNVGFVSMA KADEKGRQVL VEQIRELIMY LEKELIEKDY FGGKSVGFLD FLAGSLIPFC WEGRGLQVIT EEKFPEYNKW VKNLEKVEIV KDCIPPREKP VEHMNYMAKR IRSSL //