ID B1Y0C8_LEPCP Unreviewed; 205 AA. AC B1Y0C8; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 74. DE SubName: Full=Glutathione S-transferase domain {ECO:0000313|EMBL:ACB36607.1}; GN OrderedLocusNames=Lcho_4356 {ECO:0000313|EMBL:ACB36607.1}; OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix OS discophora (strain SP-6)). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Sphaerotilaceae; Leptothrix. OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB36607.1, ECO:0000313|Proteomes:UP000001693}; RN [1] {ECO:0000313|EMBL:ACB36607.1, ECO:0000313|Proteomes:UP000001693} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51168 / LMG 8142 / SP-6 RC {ECO:0000313|Proteomes:UP000001693}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Lykidis A., Emerson D., Richardson P.; RT "Complete sequence of Leptothrix cholodnii SP-6."; RL Submitted (MAR-2008) 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; CP001013; ACB36607.1; -; Genomic_DNA. DR RefSeq; WP_012349348.1; NC_010524.1. DR AlphaFoldDB; B1Y0C8; -. DR STRING; 395495.Lcho_4356; -. DR KEGG; lch:Lcho_4356; -. DR eggNOG; COG0625; Bacteria. DR HOGENOM; CLU_011226_6_4_4; -. DR OrthoDB; 5958450at2; -. DR Proteomes; UP000001693; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR CDD; cd03046; GST_N_GTT1_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:SF9; GLUTATHIONE S-TRANSFERASE 1; 1. DR PANTHER; PTHR44051; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001693}; KW Transferase {ECO:0000313|EMBL:ACB36607.1}. FT DOMAIN 1..81 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 86..205 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 205 AA; 23005 MW; 46D380CA602AA214 CRC64; MTLKIYGTAN SRAIRTLWAA EELGLDYEIV PLHYASDAVR SPAYLAINPN GTVPTIDDGE QVMFESLAIN LYLAKKHAPR GLWVDSMSQE AQLLQWTLWS ATEVEPLARQ WFHHSSFLPP AERQPALAEK ALEALQKRFR ILDALFATGP YLVDGRFTVA DLNLASVLLR FTDLGGGVHG HALDWHRRCM ERPAARRAFA LRQVA //