GST_SERMA
ID GST_SERMA Reviewed; 31 AA.
AC P22416;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Glutathione S-transferase GST-7.3;
DE EC=2.5.1.18;
DE Flags: Fragment;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=CIP 6755;
RX PubMed=2015287; DOI=10.1016/0167-4838(91)90050-a;
RA di Ilio C., Aceto A., Piccolomini R., Allocati N., Faraone A.,
RA Bucciarelli T., Barra D., Feferici G.;
RT "Purification and characterization of a novel glutathione transferase from
RT Serratia marcescens.";
RL Biochim. Biophys. Acta 1077:141-146(1991).
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. Beta family. {ECO:0000305}.
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DR PIR; S14727; S14727.
DR STRING; 273526.SMDB11_1495; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Transferase.
FT CHAIN 1..>31
FT /note="Glutathione S-transferase GST-7.3"
FT /id="PRO_0000185975"
FT BINDING 10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P0A9D2"
FT NON_TER 31
SQ SEQUENCE 31 AA; 3435 MW; AD993D56CD9AB0D5 CRC64;
MKLFYKAGAC SLSPHIVLRE LGLDFTAXKV D