ID   G7ZBQ9_AZOL4            Unreviewed;       235 AA.
AC   G7ZBQ9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Putative glutathione transferase {ECO:0000313|EMBL:CBS88844.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CBS88844.1};
GN   OrderedLocusNames=AZOLI_p10611 {ECO:0000313|EMBL:CBS88844.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p1 {ECO:0000313|EMBL:CBS88844.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88844.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p1 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; FQ311869; CBS88844.1; -; Genomic_DNA.
DR   RefSeq; WP_014188298.1; NC_016585.1.
DR   AlphaFoldDB; G7ZBQ9; -.
DR   KEGG; ali:AZOLI_p10611; -.
DR   HOGENOM; CLU_011226_14_4_5; -.
DR   OrthoDB; 9803562at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p1.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd10291; GST_C_YfcG_like; 1.
DR   CDD; cd03048; GST_N_Ure2p_like; 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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF19; DISULFIDE-BOND OXIDOREDUCTASE YFCG; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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:CBS88844.1};
KW   Transferase {ECO:0000313|EMBL:CBS88844.1}.
FT   DOMAIN          1..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..212
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   235 AA;  26612 MW;  4C8308A6290F30D7 CRC64;
     MIDLYFWPTP NGHKITIFLE EAGLDYRFEP VNISKGDQFK PEFLAFSPNN RMPAIIDNAP
     ADGGEPVTVF ESGAILVYLA EKTGKFLPTD LRGRKTVLEW LFWQVGGLGP MAGQNHHFVQ
     YAPERIPYAM ERYVKETGRL YGVMDKRLAD NEFLGGSELS IADMASYPWI VPHQRQQQDL
     DSFPNLKRWF NAIKERPAVV RAYEKGQAVN PSGTPTVNDE SKKILFGQSA DTVKR
//