Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

MULTISPECIES: peroxiredoxin [Pseudomonas].


LOCUS       WP_003086262             157 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_003086262
VERSION     WP_003086262.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 157)
  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 157)
  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 157)
  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 157)
  AUTHORS   Jeong,W., Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-dependent hydroperoxide peroxidase activity of
            bacterioferritin comigratory protein (BCP) as a new member of the
            thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide
            peroxidase C (AhpC) family
  JOURNAL   J Biol Chem 275 (4), 2924-2930 (2000)
   PUBMED   10644761
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 10122458
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..157
                     /product="peroxiredoxin"
                     /EC_number="1.11.1.24"
                     /GO_function="GO:0008379 - thioredoxin peroxidase activity
                     [Evidence IEA]"
                     /GO_function="GO:0051920 - peroxiredoxin activity
                     [Evidence IEA]"
                     /calculated_mol_wt=17221
     Region          7..149
                     /region_name="PRX_BCP"
                     /note="Peroxiredoxin (PRX) family, Bacterioferritin
                     comigratory protein (BCP) subfamily; composed of
                     thioredoxin-dependent thiol peroxidases, widely expressed
                     in pathogenic bacteria, that protect cells against
                     toxicity from reactive oxygen species by reducing...;
                     cd03017"
                     /db_xref="CDD:239315"
     Site            order(42,45,120)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:239315"
ORIGIN      
        1 mpvaidkpvp dftapatsgk evtlsalkgk qvvlyfypkd stpgcttegq gfrdqyaafq
       61 kantevfgis rdglkshenf kckqefpfel isdkdeavcq lfdviklkkl ygkeymgvdr
      121 stflidrdgv lrqewrgvkv pghvdavlaa aqalnga