LOCUS       WP_025242384             173 aa            linear   BCT 31-DEC-2023
DEFINITION  superoxide dismutase family protein [Stutzerimonas stutzeri].
ACCESSION   WP_025242384
VERSION     WP_025242384.1
KEYWORDS    RefSeq.
SOURCE      Stutzerimonas stutzeri (Pseudomonas stutzeri)
  ORGANISM  Stutzerimonas stutzeri
            Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
            Pseudomonadaceae; Stutzerimonas.
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 :: NF012309.4
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00080.24
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Stutzerimonas stutzeri"
                     /db_xref="taxon:316"
     Protein         1..173
                     /product="superoxide dismutase family protein"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0006801 - superoxide metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=17490
     Region          1..173
                     /region_name="Cu-Zn_Superoxide_Dismutase"
                     /note="Copper/zinc superoxide dismutase (SOD). superoxide
                     dismutases catalyse the conversion of superoxide radicals
                     to molecular oxygen. Three evolutionarily distinct
                     families of SODs are known, of which the
                     copper/zinc-binding family is one. Defects in the...;
                     cl00891"
                     /db_xref="CDD:445161"
     Site            order(29,40,42,71..73,140..141)
                     /site_type="other"
                     /note="E-class dimer interface [polypeptide binding]"
                     /db_xref="CDD:238186"
     Site            order(51,117)
                     /site_type="other"
                     /note="P-class dimer interface [polypeptide binding]"
                     /db_xref="CDD:238186"
     Site            order(67,69,92,109,112,147)
                     /site_type="active"
                     /db_xref="CDD:238186"
     Site            order(67,69,92,147)
                     /site_type="other"
                     /note="Cu2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
     Site            order(92,101,109,112)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
ORIGIN      
        1 mkqwiiaala gctamslqae tlsvpmkavt akgvgesvgt vkiesspygl vfrpelsgld
       61 sgahgfhiha kgscdpadkd getiaagaag ghwdpknagk hgepwgeghm gdlpalmvdg
      121 eghanqpvla prlkslgdik glalmvhkgg dnhsdhpqpl ggggarvacg lie
//