MULTISPECIES: peroxiredoxin [Listeria].

LOCUS       WP_003723569             181 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_003723569
VERSION     WP_003723569.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 181)
  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 181)
  AUTHORS   Copley,S.D., Novak,W.R. and Babbitt,P.C.
  TITLE     Divergence of function in the thioredoxin fold suprafamily:
            evidence for evolution of peroxiredoxins from a thioredoxin-like
            ancestor
  JOURNAL   Biochemistry 43 (44), 13981-13995 (2004)
   PUBMED   15518547
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Wood,Z.A., Schroder,E., Robin Harris,J. and Poole,L.B.
  TITLE     Structure, mechanism and regulation of peroxiredoxins
  JOURNAL   Trends Biochem Sci 28 (1), 32-40 (2003)
   PUBMED   12517450
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Aslund,F. and Beckwith,J.
  TITLE     The thioredoxin superfamily: redundancy, specificity, and gray-area
            genomics
  JOURNAL   J Bacteriol 181 (5), 1375-1379 (1999)
   PUBMED   10049365
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 10122432
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     Protein         1..181
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.-"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=20009
     Region          6..176
                     /region_name="PRX_Typ2cys"
                     /note="Peroxiredoxin (PRX) family, Typical 2-Cys PRX
                     subfamily; PRXs are thiol-specific antioxidant (TSA)
                     proteins, which confer a protective role in cells through
                     its peroxidase activity by reducing hydrogen peroxide,
                     peroxynitrite, and organic hydroperoxides; cd03015"
                     /db_xref="CDD:239313"
     Site            order(6,50..51,54,117,127,140..142,144..146,150..151,158,
                     169..172)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239313"
     Site            order(48,82..83,108,110,122)
                     /site_type="other"
                     /note="decamer (pentamer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:239313"
     Site            order(49,52,128)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239313"
     Site            order(52,169)
                     /site_type="active"
                     /note="peroxidatic and resolving cysteines [active]"
                     /db_xref="CDD:239313"
ORIGIN      
        1 maerlvgtqa prfemeavmp nqtfgkvsle knieddkwti lffypmdftf vcpteivais
       61 arsdefdaln ariigastdt ihshlawtnt pikeggigkl nyplaadtnh qvasdygvli
      121 eeegvalrgl fiinpkgeiq yevvhhnnig revdevlrvl qalqtgglcp inwqpgekti
      181 v