F4G1K5 · F4G1K5_METCR

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.

Catalytic activity

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site46Cysteine sulfenic acid (-SOH) intermediate
Active site46Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity
Binding site121substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionthioredoxin peroxidase activity
Biological Processcell redox homeostasis
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

    • Ordered locus names
      Mcup_0713

Organism names

Accessions

  • Primary accession
    F4G1K5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

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

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-158Thioredoxin

Sequence similarities

Belongs to the peroxiredoxin family. Prx6 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    215
  • Mass (Da)
    24,469
  • Last updated
    2011-06-28 v1
  • Checksum
    908708484D2579F7
MVKTYQKFPDVQVMTTAGPIDFYKDVFGKGKWLFLFAHPADFTPVCTTEFVEFAKNYSEFEKLGVQLVGLSVDSIYSHIAWLTDIEQRYGVKIPFPVIADPDKKIARLLDLIEEGSGLTVRGVFIVDPQGTIRFMALYPIEAGRNMQELIRITKALIVSYKAKVSTPVNWEPGKEVVVGAPTTLMEAEMRMKLPNSKAWYLMFKKYEELPSDQRV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002656
EMBL· GenBank· DDBJ
AEB94818.1
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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