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Database: UniProt
Entry: G7ZB30_AZOL4
LinkDB: G7ZB30_AZOL4
Original site: G7ZB30_AZOL4 
ID   G7ZB30_AZOL4            Unreviewed;       210 AA.
AC   G7ZB30;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Putative glutathione S-transferase {ECO:0000313|EMBL:CBS88403.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CBS88403.1};
GN   OrderedLocusNames=AZOLI_p10084 {ECO:0000313|EMBL:CBS88403.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p1 {ECO:0000313|EMBL:CBS88403.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88403.1, 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).
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DR   EMBL; FQ311869; CBS88403.1; -; Genomic_DNA.
DR   RefSeq; WP_014187872.1; NC_016585.1.
DR   AlphaFoldDB; G7ZB30; -.
DR   KEGG; ali:AZOLI_p10084; -.
DR   HOGENOM; CLU_011226_6_0_5; -.
DR   OMA; NYSYIAH; -.
DR   OrthoDB; 9810080at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p1.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03206; GST_C_7; 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; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR44051:SF2; HYPOTHETICAL GLUTATHIONE S-TRANSFERASE LIKE PROTEIN; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 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   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:CBS88403.1};
KW   Transferase {ECO:0000313|EMBL:CBS88403.1}.
FT   DOMAIN          7..86
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          92..210
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   210 AA;  22784 MW;  8D59DFB65A7E3D24 CRC64;
     MSTTAEPAIT LYGTPLSGHS HRVEAFLNIL GLPYRFVEAG AELRRSESFL ALNPFGQIPV
     LVDGDLVLPD SVAILVYLAD RYDASGLWNP KAPEEAARVQ RWLSVAAGDL RFGPALARIL
     TLWGGAASLT DAQAVAGRVL RFMDSHLASR DWLAAERPTI ADIACYAYVA RAPEGRIPLD
     PYPAVRRWLE RVEAIPALTP MAQSAIPQPA
//
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