superoxide dismutase family protein [Salmonella enterica].

LOCUS       WP_001035652             174 aa            linear   BCT 01-MAR-2025
ACCESSION   WP_001035652
VERSION     WP_001035652.1
KEYWORDS    RefSeq.
SOURCE      Salmonella enterica
  ORGANISM  Salmonella enterica
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Salmonella.
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 :: NF012309.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00080.25
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Salmonella enterica"
                     /db_xref="taxon:28901"
     Protein         1..174
                     /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=17864
     Region          23..174
                     /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:469976"
     Site            order(25,27,40,42,71..73,141..142)
                     /site_type="other"
                     /note="E-class dimer interface [polypeptide binding]"
                     /db_xref="CDD:238186"
     Site            order(51,118)
                     /site_type="other"
                     /note="P-class dimer interface [polypeptide binding]"
                     /db_xref="CDD:238186"
     Site            order(67,69,92,110,113,148)
                     /site_type="active"
                     /db_xref="CDD:238186"
     Site            order(67,69,92,148)
                     /site_type="other"
                     /note="Cu2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
     Site            order(92,101,110,113)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
ORIGIN      
        1 mnkklmtlav flfssaasaa stdatvnlvn angtgqkign ititeteygl lftphlsslp
       61 agihgfhihe ngscdagmkd gkpvaalaag ghldpqhtnk hlgpynpegh lgdlpalyvn
      121 qagnadypvl aprlksisqv kghaimihtg gdnhedhpnp lggggariac gvik