ID A4G970_HERAR Unreviewed; 237 AA. AC A4G970; DT 17-APR-2007, integrated into UniProtKB/TrEMBL. DT 17-APR-2007, sequence version 1. DT 27-MAR-2024, entry version 86. DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:CAL63057.1}; DE EC=2.5.1.18 {ECO:0000313|EMBL:CAL63057.1}; GN OrderedLocusNames=HEAR2945 {ECO:0000313|EMBL:CAL63057.1}; OS Herminiimonas arsenicoxydans. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Herminiimonas. OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL63057.1, ECO:0000313|Proteomes:UP000006697}; RN [1] {ECO:0000313|EMBL:CAL63057.1, 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; CAL63057.1; -; Genomic_DNA. DR AlphaFoldDB; A4G970; -. DR STRING; 204773.HEAR2945; -. DR KEGG; har:HEAR2945; -. DR eggNOG; COG0625; Bacteria. DR HOGENOM; CLU_070658_0_0_4; -. DR OrthoDB; 9799538at2; -. DR Proteomes; UP000006697; Chromosome. DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC. DR CDD; cd03194; GST_C_3; 1. DR CDD; cd03043; GST_N_1; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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; PF13409; GST_N_2; 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; PS50404; GST_NTER; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000006697}; KW Transferase {ECO:0000313|EMBL:CAL63057.1}. FT DOMAIN 22..102 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" SQ SEQUENCE 237 AA; 26235 MW; 8FB7F28C9CCDAB59 CRC64; MQTTELDPAL SQTLDSTGKN GLKLVIANKN YSSWSMRPWV AMTAFNIPFQ EVSLLLDRAD TAMQIAHYSS AGRVPILLAG ETTIWDSLAI CEYLAEQFPE KKMWPEDVAA RALARSICAE MHSGFTGVRS AMWMNIRARF PGKGRTIDAQ ADIGRISEIW ETCLALSGPS EFLFGEFSIA DAYFAPVVMR FRTYDVVLGP ALDAYVERVA AHPAVAQWIS GALAETARIP KYDVYPD //