V4JNJ9 · V4JNJ9_9CREN

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site50Cysteine sulfenic acid (-SOH) intermediate
Active site50Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity
Binding site126substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionthioredoxin peroxidase activity
Biological Processcell redox homeostasis
Biological Processcellular response to stress
Biological Processhydrogen peroxide catabolic process
Biological Processresponse to oxidative stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • ORF names
      JCHSAcid_03920

Organism names

Accessions

  • Primary accession
    V4JNJ9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

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

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-163Thioredoxin

Sequence similarities

Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Belongs to the peroxiredoxin family. Prx6 subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    228
  • Mass (Da)
    25,921
  • Last updated
    2014-01-22 v1
  • MD5 Checksum
    CFBD9AEC9EB7B9A3E009C03DF14E4FE4
MSERIPLIGEKFPEMEVVTTHGRIKLPDHFTGQGKWFILFSHPGDFTPVCTTEFYSFSRLYPEFEKLNTGLIGLSVDSNISHIEWVQWIEKNLGVKVPFPIIADPTGEVARRLGMIHPESPTAAVRAVFVVDNRGIVRAILYYPLELGRNVKEILRVVATLQAIDRTKMVAPANWPSNELIGDKMILPPPSNVADAEQRLRQYKGYAWWFTYAEAPKEEVEKVKPYAP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AYMD01000001
EMBL· GenBank· DDBJ
ESQ26740.1
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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