This section provides information on sequence similarities with other proteins and the domain(s) present in a & Domains i Domains and Repeats Feature key This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet -translational modification i This subsection of the PTM/processing section describes post-translational modifications (PTMs). Interchain (with C-52) in linked form By similarity Interchain (with C-173) in linked form By similarity This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bond i This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic i PRO_0000387961 This section describes post-translational modifications (PTMs) and/or processing / Processing i Molecule processing Feature key It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed lineage iĬellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Sauropsida › Sauria › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus This subsection of the Names and taxonomy section contains the taxonomic hierarchical classification lineage of the source organism. This is known as the 'taxonomic identifier' or 'taxid'.More.Taxonomic identifier i
This subsection of the Names and taxonomy section shows the unique identifier assigned by the NCBI to the source organism of the protein. This subsection of the Names and taxonomy section provides information on the name(s) of the organism that is the source of the protein i Search reactions for this EC number in Rhea.See the description of this EC number in ENZYME.
Search proteins in UniProtKB for this EC number.See the description of this molecule in ChEBI.Search chemical reactions in Rhea for this molecule.Search proteins in UniProtKB for this molecule.a chemical reaction that the enzyme activity i
This subsection of the Function section describes the catalytic activity of an enzyme, i.e. The disulfide is subsequently reduced by thioredoxin. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. 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 active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate.
CODE CHICKEN CORE 1.11 MANUAL
Manual assertion based on experiment in i Manually curated information for which there is published experimental evidence. Manual assertion inferred from sequence similarity to i Manually curated information which has been propagated from a related experimentally characterized protein. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (PubMed: 19766572). Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H 2O 2 (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.
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