ID E6XQF9_SHEP2 Unreviewed; 222 AA. AC E6XQF9; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 56. DE SubName: Full=Glutathione S-transferase domain protein {ECO:0000313|EMBL:ADV53783.1}; GN OrderedLocusNames=Sput200_1312 {ECO:0000313|EMBL:ADV53783.1}; OS Shewanella putrefaciens (strain 200). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=399804 {ECO:0000313|EMBL:ADV53783.1, ECO:0000313|Proteomes:UP000008209}; RN [1] {ECO:0000313|EMBL:ADV53783.1, ECO:0000313|Proteomes:UP000008209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=200 {ECO:0000313|EMBL:ADV53783.1, RC ECO:0000313|Proteomes:UP000008209}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Kolker E., Lawrence C., McCue L.A., DiChristina T., Nealson K., RA Fredrickson J.K., Woyke T.; RT "Complete sequence of Shewanella putrefaciens 200."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the GST superfamily. CC {ECO:0000256|RuleBase:RU003494}. 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; CP002457; ADV53783.1; -; Genomic_DNA. DR AlphaFoldDB; E6XQF9; -. DR KEGG; shp:Sput200_1312; -. DR PATRIC; fig|399804.5.peg.1345; -. DR HOGENOM; CLU_011226_14_4_6; -. DR OrthoDB; 9803562at2; -. DR Proteomes; UP000008209; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR CDD; cd10291; GST_C_YfcG_like; 1. DR CDD; cd03048; GST_N_Ure2p_like; 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; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1. DR PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDG01150; Main.1:_Beta-like; 1. DR SFLD; SFLDG01151; Main.2:_Nu-like; 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 3: Inferred from homology; KW Transferase {ECO:0000313|EMBL:ADV53783.1}. FT DOMAIN 1..83 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 86..216 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 222 AA; 25486 MW; 1F163CA49C3626F1 CRC64; MIDLYTAATP NGFKISIALE EMGLEYRVHK LDFSTSEQKQ PEFIAINPNG RIPAIIDRDN EDFVVFESGA ILLYLAEKTG KFLPADPKKR SQVIQWLMFQ MSGVGPMMGQ ANVFFRYFPE KIPAAIDRYQ KEGRRLFEVM NTQLATNQYL AGDEYTIADI ATWPWVRIHE WSGINMEGLT HLQRWLDELA LRPACQKGIV TPPPVEMSDE ERAKQIQKMV TK //