ID   GST_HAEIN               Reviewed;         209 AA.
AC   P44521;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
GN   Name=gst; OrderedLocusNames=HI_0111;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Beta family. {ECO:0000305}.
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DR   EMBL; L42023; AAC21788.1; -; Genomic_DNA.
DR   PIR; A64049; A64049.
DR   RefSeq; NP_438285.1; NC_000907.1.
DR   AlphaFoldDB; P44521; -.
DR   SMR; P44521; -.
DR   STRING; 71421.HI_0111; -.
DR   EnsemblBacteria; AAC21788; AAC21788; HI_0111.
DR   KEGG; hin:HI_0111; -.
DR   PATRIC; fig|71421.8.peg.115; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_2_6; -.
DR   OrthoDB; 509852at2; -.
DR   PhylomeDB; P44521; -.
DR   BioCyc; HINF71421:G1GJ1-115-MONOMER; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03188; GST_C_Beta; 1.
DR   CDD; cd03057; GST_N_Beta; 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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF10; GLUTATHIONE S-TRANSFERASE GSTA; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-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; Reference proteome; Transferase.
FT   CHAIN           1..209
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185972"
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT   DOMAIN          87..209
FT                   /note="GST C-terminal"
FT   BINDING         10
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9D2"
FT   BINDING         53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9D2"
FT   BINDING         65..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9D2"
FT   BINDING         103..106
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9D2"
SQ   SEQUENCE   209 AA;  23925 MW;  0FA44B9415B52BEA CRC64;
     MKLYGLIGAC SFVPHVALEW VKIRENADYE FEPVTRELIK SPEFLSLNPR GAVPVLVDGD
     LVLSQNQAIL HYLDELYPNS KLFGSKTVRD KAKAARWLAF FNSDVHKSFV PLFRLPNYAK
     DNETLAHTIR QQAVEQILDQ LAVANEHLES HIYFGENISV ADAYLYIMLN WCKAVKIDFS
     HLTQLSAFMQ RVETDQAVEN VRKSEELKV
//