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Database: UniProt/TrEMBL
Entry: A0A067Z2Y9_GLUOY
LinkDB: A0A067Z2Y9_GLUOY
Original site: A0A067Z2Y9_GLUOY 
ID   A0A067Z2Y9_GLUOY        Unreviewed;       228 AA.
AC   A0A067Z2Y9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Putative gluthathione S-transferase {ECO:0000313|EMBL:AHK71406.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:AHK71406.1};
GN   ORFNames=GLS_c15180 {ECO:0000313|EMBL:AHK71406.1};
OS   Gluconobacter oxydans DSM 3504.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1288313 {ECO:0000313|EMBL:AHK71406.1, ECO:0000313|Proteomes:UP000031656};
RN   [1] {ECO:0000313|EMBL:AHK71406.1, ECO:0000313|Proteomes:UP000031656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3504 {ECO:0000313|EMBL:AHK71406.1};
RX   PubMed=25267158; DOI=10.1007/s00253-014-6069-9;
RA   Kostner D., Luchterhand B., Junker A., Volland S., Daniel R., Buchs J.,
RA   Liebl W., Ehrenreich A.;
RT   "The consequence of an additional NADH dehydrogenase paralog on the growth
RT   of Gluconobacter oxydans DSM3504.";
RL   Appl. Microbiol. Biotechnol. 99:375-386(2015).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; CP004373; AHK71406.1; -; Genomic_DNA.
DR   RefSeq; WP_041112775.1; NZ_CP004373.1.
DR   AlphaFoldDB; A0A067Z2Y9; -.
DR   GeneID; 56905738; -.
DR   KEGG; goy:GLS_c15180; -.
DR   HOGENOM; CLU_011226_14_4_5; -.
DR   Proteomes; UP000031656; Chromosome.
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   Transferase {ECO:0000313|EMBL:AHK71406.1}.
FT   DOMAIN          2..89
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          92..216
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   228 AA;  26326 MW;  664B06DE171AA3E0 CRC64;
     MSDLIDLYYW PTPNGWKITI MLEELAVPYR VNLVDLVKGE QFEPAFLKLS PNNRIPALID
     PREPNEEPIS VFESGAILQY LGRKFGRFYP REERKRVEVD QWLFWQVGGL GPMAGQAHHF
     RQYAPVPIDY AIKRYTREVE RLYGVLERRL GDRKYLAGDY SVADIACIGW IVPHEKQGQH
     LGSFPRLKMW FDTVMARPAV IRGMAVGREQ REKTDLAAIA SVRGQHSP
//
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