ID   F7XHX5_SINMM            Unreviewed;       203 AA.
AC   F7XHX5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Glutathione S-transferase protein {ECO:0000313|EMBL:AEH82875.1};
GN   Name=gst15 {ECO:0000313|EMBL:AEH82875.1};
GN   OrderedLocusNames=SM11_pD0042 {ECO:0000313|EMBL:AEH82875.1};
OS   Sinorhizobium meliloti (strain SM11).
OG   Plasmid pSmeSM11d {ECO:0000313|EMBL:AEH82875.1,
OG   ECO:0000313|Proteomes:UP000009045}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH82875.1, ECO:0000313|Proteomes:UP000009045};
RN   [1] {ECO:0000313|EMBL:AEH82875.1, ECO:0000313|Proteomes:UP000009045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM11 {ECO:0000313|EMBL:AEH82875.1,
RC   ECO:0000313|Proteomes:UP000009045};
RC   PLASMID=pSmeSM11d {ECO:0000313|Proteomes:UP000009045};
RX   PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA   Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA   Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT   "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT   isolate SM11 extends the S. meliloti pan-genome.";
RL   J. Biotechnol. 155:20-33(2011).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; CP001832; AEH82875.1; -; Genomic_DNA.
DR   RefSeq; WP_003527965.1; NZ_JAJJBH010000002.1.
DR   AlphaFoldDB; F7XHX5; -.
DR   KEGG; smx:SM11_pD0042; -.
DR   PATRIC; fig|707241.3.peg.5717; -.
DR   HOGENOM; CLU_011226_6_0_5; -.
DR   Proteomes; UP000009045; Plasmid pSmeSM11d.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   CDD; cd03206; GST_C_7; 1.
DR   CDD; cd03056; GST_N_4; 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; PTHR43969; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR43969:SF9; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-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   Plasmid {ECO:0000313|EMBL:AEH82875.1}.
FT   DOMAIN          1..80
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          85..203
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   203 AA;  22356 MW;  24E112B782A77894 CRC64;
     MKLYHHPLSG HAHRARLFLS LLGIEHELVV VDFARREHKQ ADFLKLNSFG QVPVLDDAGT
     IISDSNAILV YLAKKTGRTD WLPEDAAGAA AVQRWLSVAA GQIAHGPAQA RLINVFKAPY
     RPEEVIPRSH AILALIEQEL EGRGWIAADR PTIADVALYS YVARAPEGDV DLQPYPEIRA
     WLARTEALPG FVEFEKTPVG LAA
//