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Database: UniProt/TrEMBL
Entry: D6CNI5_THIA3
LinkDB: D6CNI5_THIA3
Original site: D6CNI5_THIA3 
ID   D6CNI5_THIA3            Unreviewed;       204 AA.
AC   D6CNI5;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:CAZ90113.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CAZ90113.1};
GN   Name=gst {ECO:0000313|EMBL:CAZ90113.1};
GN   OrderedLocusNames=THI_3529 {ECO:0000313|EMBL:CAZ90113.1};
OS   Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ90113.1, ECO:0000313|Proteomes:UP000002372};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3As;
RA   Genoscope - CEA;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22701 / CIP 110005 / 3As
RC   {ECO:0000313|Proteomes:UP000002372};
RX   PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA   Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA   Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA   Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA   Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA   Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA   Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA   Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT   "Structure, function, and evolution of the Thiomonas spp. genome.";
RL   PLoS Genet. 6:E1000859-E1000859(2010).
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DR   EMBL; FP475956; CAZ90113.1; -; Genomic_DNA.
DR   RefSeq; WP_013107363.1; NZ_CTRL01000060.1.
DR   AlphaFoldDB; D6CNI5; -.
DR   KEGG; thi:THI_3529; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_1_4; -.
DR   OrthoDB; 8772754at2; -.
DR   Proteomes; UP000002372; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03188; GST_C_Beta; 1.
DR   CDD; cd03057; GST_N_Beta; 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; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF10; GLUTATHIONE S-TRANSFERASE GSTA; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-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   Reference proteome {ECO:0000313|Proteomes:UP000002372};
KW   Transferase {ECO:0000313|EMBL:CAZ90113.1}.
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          87..204
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   204 AA;  22533 MW;  2147114DB4A51AF4 CRC64;
     MKLFYSPGAC SLSPHIVLHE LGLPHDVVKV DLKTKQTSDG RDFRTINPKG YVPTLQLDDG
     TILTEGPAIV QYLADRKPEM HLAPANGTLA RYQLQEWLNF ISTELHKQFS PLFNPASSAD
     LIAAQKAKLA ERFALIAQTL EQHDYLLPSG FSVADAYLYT ILTWAGFVGV DLSPWPALVR
     YKARMEARPG VAATLAAERE AKKG
//
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