ID   PRX5_PENCI              Reviewed;         167 AA.
AC   Q9Y8B8;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Peroxiredoxin Pen c 3 {ECO:0000305};
DE            Short=Prx {ECO:0000305};
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:O43099};
DE   AltName: Full=Peroxisomal membrane protein {ECO:0000303|PubMed:10756236, ECO:0000312|EMBL:AAD42074.1};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000305};
DE            Short=TPx {ECO:0000305};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
DE   AltName: Allergen=Pen c 3 {ECO:0000303|PubMed:10756236};
OS   Penicillium citrinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5077 {ECO:0000312|EMBL:AAD42074.1};
RN   [1] {ECO:0000312|EMBL:AAD42074.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 68-78, AND ALLERGEN.
RC   STRAIN=52-5;
RX   PubMed=10756236; DOI=10.1067/mai.2000.105220;
RA   Shen H.D., Wang C.W., Chou H., Lin W.L., Tam M.F., Huang M.H., Kuo M.L.,
RA   Wang S.R., Han S.H.;
RT   "Complementary DNA cloning and immunologic characterization of a new
RT   Penicillium citrinum allergen (Pen c 3).";
RL   J. Allergy Clin. Immunol. 105:827-833(2000).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000250|UniProtKB:O43099}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000250|UniProtKB:O43099};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC       {ECO:0000250|UniProtKB:O43099}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 46% of
CC       28 Penicillium-sensitized asthmatic patients from Taipei area.
CC       {ECO:0000269|PubMed:10756236}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this typical 2-Cys
CC       Prx, C(R) is provided by the other dimeric subunit to form an
CC       intersubunit disulfide. The disulfide is subsequently reduced by
CC       thioredoxin. {ECO:0000250|UniProtKB:O43099}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF144753; AAD42074.1; -; mRNA.
DR   AlphaFoldDB; Q9Y8B8; -.
DR   SMR; Q9Y8B8; -.
DR   Allergome; 3405; Pen c 3.0101.
DR   Allergome; 523; Pen c 3.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB.
DR   CDD; cd03013; PRX5_like; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PTHR10430; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Antioxidant; Direct protein sequencing; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Redox-active center.
FT   CHAIN           1..167
FT                   /note="Peroxiredoxin Pen c 3"
FT                   /id="PRO_0000446340"
FT   DOMAIN          3..167
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        60
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:O43099"
FT   DISULFID        30
FT                   /note="Interchain (with C-60); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:O43099"
FT   DISULFID        60
FT                   /note="Interchain (with C-30); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:O43099"
SQ   SEQUENCE   167 AA;  18241 MW;  18B199A630E122B6 CRC64;
     MSLKAGDSFP EGVTFSYIPW AEDASEITSC GIPINYNASK EFANKKVVLF ALPGAFTPVC
     SANHVPEYIQ KLPELRAKGV DQVAVLAYND AYVMSAWGKA NGVTGDDILF LSDPEAKFSK
     SIGWADEEGR TYRYVLVIDN GKIIYAAKEA AKNSLELSRA DHVLKQL