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LOCUS WP_003113265 206 aa linear BCT 31-DEC-2024 ACCESSION WP_003113265 VERSION WP_003113265.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 206) AUTHORS Qi,Y. and Grishin,N.V. TITLE Structural classification of thioredoxin-like fold proteins JOURNAL Proteins 58 (2), 376-388 (2005) PUBMED 15558583 REFERENCE 2 (residues 1 to 206) 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 206) AUTHORS Nebert,D.W. and Vasiliou,V. TITLE Analysis of the glutathione S-transferase (GST) gene family JOURNAL Hum Genomics 1 (6), 460-464 (2004) PUBMED 15607001 REFERENCE 4 (residues 1 to 206) AUTHORS Sheehan,D., Meade,G., Foley,V.M. and Dowd,C.A. TITLE Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily JOURNAL Biochem J 360 (Pt 1), 1-16 (2001) PUBMED 11695986 REFERENCE 5 (residues 1 to 206) 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 10122706 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..206 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..206 /product="glutathione S-transferase" /EC_number="2.5.1.18" /GO_function="GO:0004364 - glutathione transferase activity [Evidence IEA]" /GO_function="GO:0043295 - glutathione binding [Evidence IEA]" /GO_process="GO:0042178 - xenobiotic catabolic process [Evidence IEA]" /calculated_mol_wt=23171 Region 7..79 /region_name="GST_N_3" /note="GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of...; cd03049" /db_xref="CDD:239347" Site order(15,17..18,20..21,24..25,72,75..76) /site_type="other" /note="putative C-terminal domain interface [polypeptide binding]" /db_xref="CDD:239347" Site order(15,56..58,70..71) /site_type="other" /note="putative GSH binding site (G-site) [chemical binding]" /db_xref="CDD:239347" Site order(56,69..70,72..73,76) /site_type="other" /note="putative dimer interface [polypeptide binding]" /db_xref="CDD:239347" Region 99..206 /region_name="GST_C_6" /note="C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; cd03205" /db_xref="CDD:198314" Site order(99..100,102..104,106..107,110,117..118,123,125..128, 131,134,138,141..142,145) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:198314" Site order(102,106,109..110,117,160,163..164,167,171,196, 200..201,203..206) /site_type="other" /note="N-terminal domain interface [polypeptide binding]" /db_xref="CDD:198314" Site order(106,110..111,114..115,168,171) /site_type="other" /note="putative substrate binding pocket (H-site) [chemical binding]" /db_xref="CDD:198314" ORIGIN 1 msathtlfya aaspfvrkvl vllhetgqre rvaleevtpt pvapirqlna snpagkipal 61 rlpdgqvlhd srvicdyfdq qhvgeplipr egsarwrrlt iasladavld aavlsryetf 121 vrpeekrwdt wleaqrekig rslawlegdc iaelqarfdi aaigvacalg yldlrqpewd 181 wrgryprlaa wfaevsqrps mqatra