ID GST5_CHICK Reviewed; 28 AA. AC P20137; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 28-JUN-2023, entry version 108. DE RecName: Full=Glutathione S-transferase 5; DE EC=2.5.1.18; DE AltName: Full=GST class-sigma; DE AltName: Full=GST-CL5; DE Flags: Fragment; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=2337594; DOI=10.1021/bi00455a022; RA Chang L.-H., Chuang L.-F., Tsai C.-P., Tu C.-P.D., Tam M.F.; RT "Characterization of glutathione S-transferases from day-old chick RT livers."; RL Biochemistry 29:744-750(1990). 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 -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma 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 PIR; C33948; C33948. DR AlphaFoldDB; P20137; -. DR SMR; P20137; -. DR InParanoid; P20137; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR036249; Thioredoxin-like_sf. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Reference proteome; Transferase. FT CHAIN 1..>28 FT /note="Glutathione S-transferase 5" FT /id="PRO_0000185921" FT DOMAIN 1..>28 FT /note="GST N-terminal" FT BINDING 7 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:O60760" FT NON_TER 28 SQ SEQUENCE 28 AA; 3389 MW; DA51DC0ABD203B12 CRC64; PNYKLTYFNL RGRAEISRYL FAYAGIKY //