MULTISPECIES: superoxide dismutase family protein

LOCUS       WP_000649829             175 aa            linear   BCT 01-MAR-2025
            [Enterobacteriaceae].
ACCESSION   WP_000649829
VERSION     WP_000649829.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
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..175
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..175
                     /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=18144
     Region          1..175
                     /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(52,119)
                     /site_type="other"
                     /note="P-class dimer interface [polypeptide binding]"
                     /db_xref="CDD:238186"
     Site            order(68,70,93,111,114,149)
                     /site_type="active"
                     /db_xref="CDD:238186"
     Site            order(68,70,93,149)
                     /site_type="other"
                     /note="Cu2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
     Site            order(93,102,111,114)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238186"
ORIGIN      
        1 mkckiiaaia mltaascgya aeqevpmnlv sadgkevsig kitiqetpyg llftpalhsl
       61 segihgfhvh ekgncapalk dgkpvaalsa gghfdpkntg khlgpwspdg hlgdlpalfv
      121 thdgkanypv laprlnslke ikgrslmlha ggdnhhdhpe plggggarma cgiiq