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LOCUS WP_003112753 211 aa linear BCT 01-JAN-2025 ACCESSION WP_003112753 VERSION WP_003112753.1 KEYWORDS RefSeq. SOURCE Pseudomonas aeruginosa ORGANISM Pseudomonas aeruginosa Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas. REFERENCE 1 (residues 1 to 211) AUTHORS Frova,C. TITLE Glutathione transferases in the genomics era: new insights and perspectives JOURNAL Biomol Eng 23 (4), 149-169 (2006) PUBMED 16839810 REFERENCE 2 (residues 1 to 211) AUTHORS Hayes,J.D., Flanagan,J.U. and Jowsey,I.R. TITLE Glutathione transferases JOURNAL Annu Rev Pharmacol Toxicol 45, 51-88 (2005) PUBMED 15822171 REFERENCE 3 (residues 1 to 211) AUTHORS Armstrong,R.N. TITLE Structure, catalytic mechanism, and evolution of the glutathione transferases JOURNAL Chem Res Toxicol 10 (1), 2-18 (1997) PUBMED 9074797 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10122607 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..211 /organism="Pseudomonas aeruginosa" /db_xref="taxon:287" Protein 1..211 /product="glutathione S-transferase family protein" /EC_number="2.5.1.-" /GO_function="GO:0004364 - glutathione transferase activity [Evidence IEA]" /GO_process="GO:0006749 - glutathione metabolic process [Evidence IEA]" /calculated_mol_wt=23658 Region 4..76 /region_name="GST_N_1" /note="GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with...; cd03043" /db_xref="CDD:239341" Site order(15,17..18,20..21,24..25,69,72..73) /site_type="other" /note="putative C-terminal domain interface [polypeptide binding]" /db_xref="CDD:239341" Site order(15,54..56,67..68) /site_type="other" /note="putative GSH binding site (G-site) [chemical binding]" /db_xref="CDD:239341" Site order(54,66..67,69..70,73) /site_type="other" /note="putative dimer interface [polypeptide binding]" /db_xref="CDD:239341" Region 89..203 /region_name="GST_C_3" /note="C-terminal, alpha helical domain of an unknown subfamily 3 of Glutathione S-transferases; cd03194" /db_xref="CDD:198303" Site order(92,99,161,164..165,168,172) /site_type="other" /note="putative N-terminal domain interface [polypeptide binding]" /db_xref="CDD:198303" Site order(92..93,96..97,100,136) /site_type="other" /note="putative dimer interface [polypeptide binding]" /db_xref="CDD:198303" Site order(99,103..104,107..108,169,172) /site_type="other" /note="putative substrate binding pocket (H-site) [chemical binding]" /db_xref="CDD:198303" ORIGIN 1 maltivignr ndsswslrgw lalrmsgaaf deilvplgrp dtrerilqys ptgkvpllks 61 edgdiwdsla iaeylaerfp eahlwprgea aralarsvca emhsgfaalr gelpmdlrrq 121 qplvelseat rqdiqricea wadclrrfgq dgpflfghas ladafyapva arfrsyavel 181 pdiartyvet iyqwpafraw ydaalreqag s