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Database: UniProt
Entry: G7FYL8_9GAMM
LinkDB: G7FYL8_9GAMM
Original site: G7FYL8_9GAMM 
ID   G7FYL8_9GAMM            Unreviewed;       224 AA.
AC   G7FYL8;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:GAA78241.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:GAA78241.1};
GN   Name=gst {ECO:0000313|EMBL:GAA78241.1};
GN   ORFNames=P20495_0732 {ECO:0000313|EMBL:GAA78241.1};
OS   Pseudoalteromonas sp. BSi20495.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA78241.1, ECO:0000313|Proteomes:UP000003050};
RN   [1] {ECO:0000313|Proteomes:UP000003050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX   PubMed=22275105; DOI=10.1128/JB.06427-11;
RA   Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT   ice.";
RL   J. Bacteriol. 194:908-909(2012).
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:GAA78241.1}.
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DR   EMBL; BADY01000024; GAA78241.1; -; Genomic_DNA.
DR   RefSeq; WP_008134283.1; NZ_BADY01000024.1.
DR   AlphaFoldDB; G7FYL8; -.
DR   Proteomes; UP000003050; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00299; GST_C_family; 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; 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   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-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   Transferase {ECO:0000313|EMBL:GAA78241.1}.
FT   DOMAIN          4..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          92..215
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   224 AA;  24994 MW;  A3224E601B9AAE0F CRC64;
     MTDAQLTLIS HPLCPFVQRA AIVLMEKNVP FERINVDLSA KPDWFLALSP LGKVPLLKIS
     QTDNSEAIIF ESMVICEYLE ESQSGADLYP IDALAKAQQR GWVEFGSSTL TEAWQFLNAK
     DSFIADSKQT AFRNKLKQLE AVLTEGPYFN GTSFGMVDAV FAPIFRYFDL LNPTVSQPIF
     ENLPRVTAWR VALASRESVI AAVSVDYAEQ FQQHLVKQQA LLAG
//
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