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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//