ID   GST_XANCP               Reviewed;         204 AA.
AC   P45875;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Glutathione S-transferase GST-4.5;
DE            EC=2.5.1.18;
GN   Name=gst; OrderedLocusNames=XCC0929;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-32.
RX   PubMed=8342943; DOI=10.1006/abbi.1993.1399;
RA   di Ilio C., Aceto A., Allocati N., Piccolomini R., Bucciarelli T.,
RA   Dragani B., Faraone A., Sacchetta P., Petruzzelli R., Federici G.;
RT   "Characterization of glutathione transferase from Xanthomonas campestris.";
RL   Arch. Biochem. Biophys. 305:110-114(1993).
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. {ECO:0000305}.
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DR   EMBL; AE008922; AAM40239.1; -; Genomic_DNA.
DR   PIR; S35583; S35583.
DR   RefSeq; NP_636315.1; NC_003902.1.
DR   RefSeq; WP_011036143.1; NC_003902.1.
DR   AlphaFoldDB; P45875; -.
DR   SMR; P45875; -.
DR   STRING; 340.xcc-b100_3425; -.
DR   EnsemblBacteria; AAM40239; AAM40239; XCC0929.
DR   KEGG; xcc:XCC0929; -.
DR   PATRIC; fig|190485.4.peg.1001; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_1_6; -.
DR   OMA; ESHIYFG; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Reference proteome; Transferase.
FT   CHAIN           1..204
FT                   /note="Glutathione S-transferase GST-4.5"
FT                   /id="PRO_0000185976"
FT   DOMAIN          1..77
FT                   /note="GST N-terminal"
FT   DOMAIN          83..204
FT                   /note="GST C-terminal"
FT   BINDING         10
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..62
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        22
FT                   /note="C -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="E -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  22321 MW;  F6302C321EB1F86F CRC64;
     MKLYTKPGAC SLADHIVLRW SCLPFELTVV DAATMKSPDY LRLNPAGAVP LLVVDQWALT
     QNAAILNYIA DTAPLTGLGG DGTARSRAEI NRWIAFVNAD LHPTFKPLFG STAYLQEDAL
     IQRSHEDART KLRTLYTRVD AHLQGRNWLA GDTHTGADAY LFVTLRWAHK AGVDLSGLSA
     LDAFFQRMLA DADVQAALQA EGLN