P95895 · TDXH_SACS2

Function

function

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule.

Catalytic activity

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site49Cysteine sulfenic acid (-SOH) intermediate
Binding site125substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionthioredoxin-dependent peroxiredoxin activity
Biological Processcell redox homeostasis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxiredoxin
  • EC number
  • Alternative names
    • Thioredoxin-dependent peroxiredoxin

Gene names

    • ORF names
      C02015, C02_016
    • Ordered locus names
      SSO2121

Organism names

Accessions

  • Primary accession
    P95895

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001351691-215Peroxiredoxin

Proteomic databases

Interaction

Subunit

Homodecamer. Pentamer of dimers that assemble into a ring structure.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-162Thioredoxin

Sequence similarities

Belongs to the peroxiredoxin family. Prx6 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    215
  • Mass (Da)
    24,745
  • Last updated
    1997-05-01 v1
  • Checksum
    5210477EF4C9607B
MSEERIPLIGERFPEMEVITTQGRIKLPDDYKGRWFVLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSNISHIEWIMWIEKNLKVEIPFPIIADPMGNVAKRLGMIHAQSSTATVRAVFVVDDKGVVRLILYYPMEIGRNIDEILRAIRALQLVDKAGVVTPANWPNNELIGDKVINPAPRTIKDAKMRLGQPFDWWFTYKEVKTT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y08256
EMBL· GenBank· DDBJ
CAA69447.1
EMBL· GenBank· DDBJ
Genomic DNA
AE006641
EMBL· GenBank· DDBJ
AAK42300.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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