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Database: UniProt
Entry: A0A150UKY4_9BRAD
LinkDB: A0A150UKY4_9BRAD
Original site: A0A150UKY4_9BRAD 
ID   A0A150UKY4_9BRAD        Unreviewed;       225 AA.
AC   A0A150UKY4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KYG24797.1};
GN   ORFNames=SE92_02430 {ECO:0000313|EMBL:KYG24797.1};
OS   Bradyrhizobium sp. AT1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=574934 {ECO:0000313|EMBL:KYG24797.1, ECO:0000313|Proteomes:UP000075342};
RN   [1] {ECO:0000313|EMBL:KYG24797.1, ECO:0000313|Proteomes:UP000075342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT1 {ECO:0000313|EMBL:KYG24797.1,
RC   ECO:0000313|Proteomes:UP000075342};
RA   Okubo T., Minamisawa K.;
RT   "Evolution of nitrogen fixation genes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000710};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYG24797.1}.
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DR   EMBL; JXDL01000001; KYG24797.1; -; Genomic_DNA.
DR   RefSeq; WP_063203304.1; NZ_JXDL01000001.1.
DR   AlphaFoldDB; A0A150UKY4; -.
DR   STRING; 574934.SE92_02430; -.
DR   PATRIC; fig|574934.3.peg.506; -.
DR   OrthoDB; 9813092at2; -.
DR   Proteomes; UP000075342; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:UniProt.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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; IPR005442; GST_omega.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43968; -; 1.
DR   PANTHER; PTHR43968:SF15; GLUTATHIONE TRANSFERASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transferase {ECO:0000313|EMBL:KYG24797.1}.
FT   DOMAIN          3..85
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   225 AA;  25174 MW;  B7EEBB17446C5EF7 CRC64;
     MTASLKLISH KLCPYVQRAV IALKEKDVPF ERIDIDLANK PEWFLKLSPL GKVPVLVVTT
     DKGEVALFES NVICEYIEET QGGAKLHPAD PLKRAEHRAW MEFGSAILGD LWGLETTADP
     ATFESKRQAL AAKFARVEAA LGAGPFFSGE QFSLVDAVFA PIFRYFDLFD ELTEHGIFRD
     VPKVRAWRAE LARRPSVRTA VGTDYPQLLR AFLVRHDAHL LKLAA
//
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