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Database: UniProt/TrEMBL
Entry: I3V1C7_PSEPU
LinkDB: I3V1C7_PSEPU
Original site: I3V1C7_PSEPU 
ID   I3V1C7_PSEPU            Unreviewed;       227 AA.
AC   I3V1C7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Glutathione S-transferase domain-containing protein {ECO:0000313|EMBL:AFK71548.1};
GN   ORFNames=YSA_08833 {ECO:0000313|EMBL:AFK71548.1};
OS   Pseudomonas putida ND6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK71548.1, ECO:0000313|Proteomes:UP000005268};
RN   [1] {ECO:0000313|EMBL:AFK71548.1, ECO:0000313|Proteomes:UP000005268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND6 {ECO:0000313|EMBL:AFK71548.1,
RC   ECO:0000313|Proteomes:UP000005268};
RX   PubMed=22933774; DOI=10.1128/JB.01190-12;
RA   Li S., Zhao H., Li Y., Niu S., Cai B.;
RT   "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT   Strain ND6.";
RL   J. Bacteriol. 194:5154-5155(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};
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DR   EMBL; CP003588; AFK71548.1; -; Genomic_DNA.
DR   RefSeq; WP_014755986.1; NC_017986.1.
DR   AlphaFoldDB; I3V1C7; -.
DR   KEGG; ppi:YSA_08833; -.
DR   HOGENOM; CLU_011226_9_3_6; -.
DR   Proteomes; UP000005268; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00299; GST_C_family; 1.
DR   CDD; cd00570; GST_N_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:AFK71548.1}.
FT   DOMAIN          3..86
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          91..213
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   227 AA;  25614 MW;  B7F14F68C7041C64 CRC64;
     MPNNLKLVSH GLCPFVQRVA IALLEKNIAF ERETIDLANK PEWFLAISPS GKVPLLIVGE
     EEESQTVLFE SFPICEFIED EYRQVPLHPT VPLKRAKHRA WMEFSTAAMG DAWGMINSTD
     KEGFVHKASE LRGKLMKLDS ALVAGPYFEG AEFSMVDVVM APIFRFFEVL NSPVHNVVLD
     GLPRVEAWRQ SLMTRPSVRQ AVSADYSENL RKFLIDRSAY VVSDCPV
//
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