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Database: UniProt/TrEMBL
Entry: A4G202_HERAR
LinkDB: A4G202_HERAR
Original site: A4G202_HERAR 
ID   A4G202_HERAR            Unreviewed;       202 AA.
AC   A4G202;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Glutathione S-transferase (GST-like protein) {ECO:0000313|EMBL:CAL60539.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CAL60539.1};
GN   OrderedLocusNames=HEAR0313 {ECO:0000313|EMBL:CAL60539.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60539.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL60539.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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DR   EMBL; CU207211; CAL60539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G202; -.
DR   STRING; 204773.HEAR0313; -.
DR   KEGG; har:HEAR0313; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_12_2_4; -.
DR   OrthoDB; 8634103at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03205; GST_C_6; 1.
DR   CDD; cd03049; GST_N_3; 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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW   Transferase {ECO:0000313|EMBL:CAL60539.1}.
FT   DOMAIN          1..78
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          83..202
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   202 AA;  22783 MW;  9C9227B2D43290D8 CRC64;
     MKLIGSLASP YVRKVRVVML EKKIDYDFVL ENVWSPDTLI QESNPLGKVP CLVMEDGGAM
     FDSRVIVEYL DTLTPVGKLI PAHGRERAEV KCWEALADGV CDAAMLLRLE HTLRPAEQRS
     QSWIDRQTAK VNAGLKAMST GLKDTAFCAG NQYTLADVAV GCTLEWLTFR FPEITWRTEY
     PNLEKMLEKL SERPSFKETS PK
//
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