P0C5C8 · REHYA_ORYSI

Function

function

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity).
Seems to contribute to the inhibition of germination during stress (By similarity).

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.

TypeIDPosition(s)Description
Active site46Cysteine sulfenic acid (-SOH) intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionthioredoxin-dependent peroxiredoxin activity

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    1-Cys peroxiredoxin A
  • EC number
  • Short names
    1-Cys Prx A
  • Alternative names
    • Protein RAB24
    • Rice 1Cys-peroxiredoxin (R1C-Prx)
    • Thioredoxin peroxidase A
    • Thioredoxin-dependent peroxiredoxin A

Gene names

    • ORF names
      OsI_27030

Organism names

  • Taxonomic identifier
  • Strains
    • cv. 93-11
    • cv. Guang-Lu-Ai No.4
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    P0C5C8
  • Secondary accessions
    • A2YP41
    • A3BMM5
    • B8B525
    • P52573
    • Q0D4A2
    • Q8GVH0

Proteomes

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Protein family/group databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003002601-2201-Cys peroxiredoxin A

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain4-165Thioredoxin
Motif195-218Bipartite nuclear localization signal

Sequence similarities

Belongs to the peroxiredoxin family. Prx6 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    220
  • Mass (Da)
    24,072
  • Last updated
    2007-09-11 v1
  • Checksum
    317D9D76C7D63F1D
MPGLTIGDTVPNLELDSTHGKIRIHDFVGDTYIILFSHPGDFTPVCTTELAAMAGYAKEFDKRGVKLLGISCDDVQSHKDWIKDIEAYKPGNRVTYPIMADPSREAIKQLNMVDPDEKDSNGGHLPSRALHIVGPDKKVKLSFLYPSCVGRNMDEVVRAVDALQTAAKHAVATPVNWKPGERVVIPPGVSDDEAKEKFPQGFDTADLPSGKGYLRFTKVG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM000132
EMBL· GenBank· DDBJ
EEC82522.1
EMBL· GenBank· DDBJ
Genomic DNA
CT830870
EMBL· GenBank· DDBJ
-mRNA No translation available.

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp