MULTISPECIES: glutathione S-transferase [Klebsiella].

LOCUS       WP_004151669             201 aa            linear   BCT 31-MAR-2023
ACCESSION   WP_004151669
VERSION     WP_004151669.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 201)
  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 201)
  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 201)
  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
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 10600528
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..201
                     /product="glutathione S-transferase"
                     /EC_number="2.5.1.18"
                     /GO_function="GO:0043295 - glutathione binding [Evidence
                     IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=22144
     Region          3..71
                     /region_name="GST_N_3"
                     /note="Glutathione S-transferase, N-terminal domain;
                     pfam13417"
                     /db_xref="CDD:433190"
     Site            order(11,13..14,16..17,20..21,64,67..68)
                     /site_type="other"
                     /note="C-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:238319"
     Site            order(11,48..50,62..63)
                     /site_type="other"
                     /note="GSH binding site (G-site) [chemical binding]"
                     /db_xref="CDD:238319"
     Site            order(48,61..62,64..65,68)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238319"
     Region          92..199
                     /region_name="GST_C_family"
                     /note="C-terminal, alpha helical domain of the Glutathione
                     S-transferase family; cl02776"
                     /db_xref="CDD:470672"
     Site            order(92,99,154,157..158,161,165)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198286"
     Site            order(92..93,96..97,100,134)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198286"
     Site            order(99,102..103,162,165)
                     /site_type="other"
                     /note="substrate binding pocket (H-site) [chemical
                     binding]"
                     /db_xref="CDD:198286"
ORIGIN      
        1 mkligmmdsp yvrrvavsla lygvefeslp lsvfsgfdef srinpvvkap tvvldngtql
       61 mdstlilhyf ettnpagrrl lpvhpealar dlhllgvila acekavqhvy ehrlrpeekq
      121 hqpwiarvtg qllaacrewd arladraaaa qpdqvlvtst vvwsfiqlmi pavvsaaafp
      181 hiralaekge alpafqqypl g