Grx4 family monothiol glutaredoxin [Grimontia hollisae].

LOCUS       WP_005503392             112 aa            linear   BCT 28-FEB-2022
ACCESSION   WP_005503392
VERSION     WP_005503392.1
KEYWORDS    RefSeq.
SOURCE      Grimontia hollisae
  ORGANISM  Grimontia hollisae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Grimontia.
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  :: HMM
            Evidence Accession :: NF008086.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK10824
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Grimontia hollisae"
                     /db_xref="taxon:673"
     Protein         1..112
                     /product="Grx4 family monothiol glutaredoxin"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=12515
     Region          1..105
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Site            order(21,29..31,69..70)
                     /site_type="other"
                     /note="putative GSH binding site [chemical binding]"
                     /db_xref="CDD:239326"
     Site            order(29,32)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239326"
ORIGIN      
        1 metidkikqq ieenpillym kgspklpscg fssqasqalm acgekfayvd ilqnpdirae
       61 lpiyaqwptf pqlwvegeli ggcdiilemf qkgelqplik naaarrdmed nn