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UniProtKB - P0A251 (AHPC_SALTY)

Entry version 115 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Alkyl hydroperoxide reductase C

Gene

ahpC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.2 Publications

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 typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by AhpF.1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 55.1 sec(-1) with H2O2 as substrate.1 Publication
  1. KM=1.4 µM for H2O21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei47Cysteine sulfenic acid (-SOH) intermediate1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAntioxidant, Oxidoreductase, Peroxidase

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.11.1.15, 5542

    Protein family/group databases

    PeroxiBase, a peroxidase database

    More...    PeroxiBasei    		4829, SetypAhpC

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Alkyl hydroperoxide reductase C1 Publication (EC:1.11.1.261 Publication)
    Alternative name(s):
    Alkyl hydroperoxide reductase protein C221 Publication
    Peroxiredoxin
    Thioredoxin peroxidase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:ahpC1 Publication
    Ordered Locus Names:STM0608
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri99287 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Salmonella ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001014 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001351202 – 187Alkyl hydroperoxide reductase CAdd BLAST186

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi47Interchain (with C-166); in linked formCombined sources1 Publication
    Disulfide bondi166Interchain (with C-47); in linked formCombined sources1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P0A251

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer; disulfide-linked, upon oxidation (PubMed:2643600, PubMed:8555198). 5 homodimers assemble to form a ring-like decamer (PubMed:11969410).

    3 Publications

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1187
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P0A251

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P0A251

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 157ThioredoxinPROSITE-ProRule annotationAdd BLAST156

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_042529_21_3_6

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		FWYPKDF

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P0A251

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.40.30.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR017559, AhpC
    IPR000866, AhpC/TSA
    IPR024706, Peroxiredoxin_AhpC-typ
    IPR019479, Peroxiredoxin_C
    IPR036249, Thioredoxin-like_sf
    IPR013766, Thioredoxin_domain

    The PANTHER Classification System

    More...    PANTHERi    		PTHR10681:SF121, PTHR10681:SF121, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF10417, 1-cysPrx_C, 1 hit
    PF00578, AhpC-TSA, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF000239, AHPC, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF52833, SSF52833, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR03137, AhpC, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS51352, THIOREDOXIN_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A251-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE 
            60         70         80         90        100
    LGDVADHYEE LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP 
           110        120        130        140        150
    TGALTRNFDN MREDEGLADR ATFVVDPQGI IQAIEVTAEG IGRDASDLLR 
           160        170        180 
    KIKAAQYVAA HPGEVCPAKW KEGEATLAPS LDLVGKI
    Length:187
    Mass (Da):20,747
    Last modified:January 23, 2007 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i83B251C74DE9860D
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2S → G AA sequence (PubMed:2643600).Curated1
    Sequence conflicti5N → D AA sequence (PubMed:2643600).Curated1
    Sequence conflicti14Q → N AA sequence (PubMed:2643600).Curated1
    Sequence conflicti17K → H AA sequence (PubMed:2643600).Curated1
    Sequence conflicti20E → H AA sequence (PubMed:2643600).Curated1
    Sequence conflicti23E → S AA sequence (PubMed:2643600).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		J05478 Unassigned DNA Translation: AAA16431.1
    AE006468 Genomic DNA Translation: AAL19559.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A35441

    NCBI Reference Sequences

    More...    RefSeqi    		NP_459600.1, NC_003197.2
    WP_000052802.1, NC_003197.2

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAL19559; AAL19559; STM0608

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		1252128
    57493531

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		stm:STM0608

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|99287.12.peg.640

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		J05478 Unassigned DNA Translation: AAA16431.1
    AE006468 Genomic DNA Translation: AAL19559.1
    PIRiA35441
    RefSeqiNP_459600.1, NC_003197.2
    WP_000052802.1, NC_003197.2

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1N8JX-ray2.17A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-187[»]
    1YEPX-ray2.50A/B/C/D/E2-187[»]
    1YEXX-ray2.30A/B/C/D/E2-187[»]
    1YF0X-ray2.50A/B/C/D/E2-187[»]
    1YF1X-ray2.60A/B/C/D/E/F/G/H/I/J2-187[»]
    3EMPX-ray4.00A/B/C/D/E2-187[»]
    4MA9X-ray1.82A/B/C/D/E2-187[»]
    4MABX-ray1.90A/B/C/D/E2-187[»]
    4XRAX-ray1.75A/B/C/D/E2-187[»]
    4XRDX-ray2.30A/B/C/D/E2-187[»]
    4XS1X-ray2.10A/B/C/D/E2-187[»]
    4XS4X-ray2.65A/B/C/D/E2-187[»]
    4XS6X-ray3.35A/B/C/D/E2-187[»]
    4XTSX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T2-187[»]
    5UKAX-ray1.90A/B/C/D/E2-187[»]
    SMRiP0A251
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    PeroxiBasei4829, SetypAhpC

    Proteomic databases

    PaxDbiP0A251

    Genome annotation databases

    EnsemblBacteriaiAAL19559; AAL19559; STM0608
    GeneIDi1252128
    57493531
    KEGGistm:STM0608
    PATRICifig|99287.12.peg.640

    Phylogenomic databases

    HOGENOMiCLU_042529_21_3_6
    OMAiFWYPKDF
    PhylomeDBiP0A251

    Enzyme and pathway databases

    BRENDAi1.11.1.15, 5542

    Miscellaneous databases

    EvolutionaryTraceiP0A251

    Family and domain databases

    Gene3Di3.40.30.10, 1 hit
    InterProiView protein in InterPro
    IPR017559, AhpC
    IPR000866, AhpC/TSA
    IPR024706, Peroxiredoxin_AhpC-typ
    IPR019479, Peroxiredoxin_C
    IPR036249, Thioredoxin-like_sf
    IPR013766, Thioredoxin_domain
    PANTHERiPTHR10681:SF121, PTHR10681:SF121, 1 hit
    PfamiView protein in Pfam
    PF10417, 1-cysPrx_C, 1 hit
    PF00578, AhpC-TSA, 1 hit
    PIRSFiPIRSF000239, AHPC, 1 hit
    SUPFAMiSSF52833, SSF52833, 1 hit
    TIGRFAMsiTIGR03137, AhpC, 1 hit
    PROSITEiView protein in PROSITE
    PS51352, THIOREDOXIN_2, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAHPC_SALTY
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A251
    Secondary accession number(s): P19479
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: January 23, 2007
    Last modified: April 7, 2021
    This is version 115 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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