ID GSTX1_NICPL Reviewed; 219 AA. AC P50471; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 86. DE RecName: Full=Probable glutathione S-transferase MSR-1; DE EC=2.5.1.18; DE AltName: Full=Auxin-regulated protein MSR-1; GN Name=MSR-1; OS Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4092; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1498603; DOI=10.1105/tpc.4.4.451; RA Dominov J.A., Stenzler L., Lee S., Schwarz J.J., Leisner S., Howell S.H.; RT "Cytokinins and auxins control the expression of a gene in Nicotiana RT plumbaginifolia cells by feedback regulation."; RL Plant Cell 4:451-461(1992). CC -!- FUNCTION: May play an important role in hormonal and growth regulatory CC responses. 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 -!- INDUCTION: By auxin and cytokinin. CC -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family. CC {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; S44036; AAB47712.2; -; mRNA. DR PIR; JQ1606; JQ1606. DR AlphaFoldDB; P50471; -. DR SMR; P50471; -. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro. 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; IPR004046; GST_C. DR InterPro; IPR045074; GST_C_Tau. DR InterPro; IPR045073; Omega/Tau-like. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11260:SF781; GLUTATHIONE S-TRANSFERASE U22; 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; 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 2: Evidence at transcript level; KW Auxin signaling pathway; Transferase. FT CHAIN 1..219 FT /note="Probable glutathione S-transferase MSR-1" FT /id="PRO_0000185862" FT DOMAIN 4..83 FT /note="GST N-terminal" FT DOMAIN 89..208 FT /note="GST C-terminal" FT BINDING 14 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 41 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 55 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 67..68 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" SQ SEQUENCE 219 AA; 25269 MW; DCE165B0FB33A759 CRC64; MESNNVVLLD FSGSSFGMRL RIALALKGIK YEAKEENLSD KSPLLLEMNP VHKKIPILIH NGKPICESLN ILEYIDEVWH EKCPLLPSDP YQRSQARFWA NYIDNKIYST GRRVWSGKGE DQEEAKKEFI EIFKTLEGEL GNKTYFGGDN LGFVDVALVP FTSWFYSYET CANFSIEAEC RKLVVWQNCM ENERVSKSLP HPHKIYDFVL ELKHKLGLA //