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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//