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Protein

Peroxiredoxin Asp f3

Gene

aspf3

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 and as sensor of hydrogen peroxide-mediated signaling events. Required for virulence.1 Publication

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 Prx, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Kineticsi

kcat is 12.53 sec(-1) with H2O2 as substrate and 12.96 sec(-1) with tert-butyl hydroperoxide as substrate.1 Publication
  1. KM=72.29 µM for H2O21 Publication
  2. KM=70.48 µM for tert-butyl hydroperoxide1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei61Cysteine sulfenic acid (-SOH) intermediate1 Publication1

    GO - Molecular functioni

    • IgE binding Source: AspGD
    • peroxidase activity Source: UniProtKB-KW
    • peroxiredoxin activity Source: UniProtKB-EC

    GO - Biological processi

    Keywordsi

    Molecular functionAntioxidant, Oxidoreductase, Peroxidase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxiredoxin Asp f3Curated (EC:1.11.1.151 Publication)
    Short name:
    Prx
    Alternative name(s):
    Thioredoxin peroxidase
    Short name:
    TPx
    Allergen: Asp f 3
    Gene namesi
    Name:aspf31 Publication
    ORF Names:AFUA_6G02280
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    Proteomesi
    • UP000002530 Componenti: Chromosome 6

    Organism-specific databases

    EuPathDBiFungiDB:Afu6g02280.

    Subcellular locationi

    Pathology & Biotechi

    Allergenic propertiesi

    Causes an allergic reaction in human. Shares common IgE-binding epitopes with allergen Cand b 2 of Candida boidinii.1 Publication

    Disruption phenotypei

    Renders cells sensitive to reactive oxigen species. Renders A.fumigatus avirulent in a mouse model of pulmonary aspergillosis.1 Publication

    Keywords - Diseasei

    Allergen

    Protein family/group databases

    Allergomei3121. Asp f 3.0101.
    73. Asp f 3.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000566031 – 168Peroxiredoxin Asp f3Add BLAST168

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi31Interchain (with C-61); in linked form1 Publication
    Disulfide bondi61Interchain (with C-31); in linked form1 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiO43099.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked, upon oxidation.1 Publication

    GO - Molecular functioni

    • IgE binding Source: AspGD

    Protein-protein interaction databases

    STRINGi5085.CADAFUBP00009334.

    Structurei

    Secondary structure

    1168
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi15 – 18Combined sources4
    Helixi23 – 25Combined sources3
    Beta strandi35 – 38Combined sources4
    Helixi39 – 42Combined sources4
    Turni43 – 45Combined sources3
    Beta strandi46 – 52Combined sources7
    Helixi59 – 63Combined sources5
    Helixi65 – 78Combined sources14
    Beta strandi83 – 90Combined sources8
    Helixi92 – 101Combined sources10
    Beta strandi108 – 113Combined sources6
    Helixi115 – 117Combined sources3
    Helixi118 – 122Combined sources5
    Beta strandi134 – 140Combined sources7
    Beta strandi143 – 149Combined sources7
    Helixi161 – 165Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5J9BX-ray2.10A/B2-168[»]
    5J9CX-ray1.96A/B2-168[»]
    ProteinModelPortaliO43099.
    SMRiO43099.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini4 – 158ThioredoxinAdd BLAST155

    Sequence similaritiesi

    Belongs to the peroxiredoxin family. Prx5 subfamily.Curated

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    HOGENOMiHOG000255884.
    InParanoidiO43099.
    KOiK14171.
    OMAiVFSYIPW.
    OrthoDBiEOG092C4YDK.

    Family and domain databases

    InterProiView protein in InterPro
    IPR013740. Redoxin.
    IPR036249. Thioredoxin-like_sf.
    IPR013766. Thioredoxin_domain.
    PfamiView protein in Pfam
    PF08534. Redoxin. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiView protein in PROSITE
    PS51352. THIOREDOXIN_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O43099-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSGLKAGDSF PSDVVFSYIP WSEDKGEITA CGIPINYNAS KEWADKKVIL
    60 70 80 90 100
    FALPGAFTPV CSARHVPEYI EKLPEIRAKG VDVVAVLAYN DAYVMSAWGK
    110 120 130 140 150
    ANQVTGDDIL FLSDPDARFS KSIGWADEEG RTKRYALVID HGKITYAALE
    160
    PAKNHLEFSS AETVLKHL
    Length:168
    Mass (Da):18,453
    Last modified:June 1, 1998 - v1
    Checksum:iAFFCD72C5A1CCBB2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U58050 mRNA. Translation: AAB95638.1.
    AAHF01000012 Genomic DNA. Translation: EAL85811.1.
    RefSeqiXP_747849.1. XM_742756.1.

    Genome annotation databases

    GeneIDi3505266.
    KEGGiafm:AFUA_6G02280.

    Similar proteinsi

    Entry informationi

    Entry nameiPRX5_ASPFU
    AccessioniPrimary (citable) accession number: O43099
    Secondary accession number(s): Q4WCS7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: November 22, 2017
    This is version 109 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Allergens
      Nomenclature of allergens and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families