ID   MALF2_MALFU             Reviewed;         177 AA.
AC   P56577;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Putative peroxiredoxin;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P38013};
DE   AltName: Full=MF1;
DE   AltName: Full=Thioredoxin reductase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000305};
DE   AltName: Allergen=Mal f 2;
OS   Malassezia furfur (Pityriasis versicolor infection agent) (Pityrosporum
OS   furfur).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=55194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TIMM 2782;
RX   PubMed=9675120; DOI=10.1006/bbrc.1998.8944;
RA   Yasueda H., Hashida-Okado T., Saito A., Uchida K., Kuroda M., Onishi Y.,
RA   Takahashi K., Yamaguchi H., Takesako K., Akiyama K.;
RT   "Identification and cloning of two novel allergens from the lipophilic
RT   yeast, Malassezia furfur.";
RL   Biochem. Biophys. Res. Commun. 248:240-244(1998).
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:P38013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol +
CC         [thioredoxin]-disulfide + 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:P38013};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC       {ECO:0000250|UniProtKB:P38013}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000269|PubMed:9675120}.
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:P38013}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB011804; BAA32435.1; -; Genomic_DNA.
DR   PIR; JE0226; JE0226.
DR   AlphaFoldDB; P56577; -.
DR   SMR; P56577; -.
DR   Allergome; 3361; Mala f 2.0101.
DR   Allergome; 468; Mala f 2.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0005777; C:peroxisome; IEA:TreeGrafter.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; ISS:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   CDD; cd03013; PRX5_like; 1.
DR   FunFam; 3.40.30.10:FF:000020; Peroxiredoxin; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR   PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Allergen; Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..177
FT                   /note="Putative peroxiredoxin"
FT                   /id="PRO_0000056606"
FT   DOMAIN          8..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           175..177
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        64
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P38013"
FT   DISULFID        34
FT                   /note="Interchain (with C-64); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P38013"
FT   DISULFID        64
FT                   /note="Interchain (with C-34); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P38013"
SQ   SEQUENCE   177 AA;  19193 MW;  1E1F907C68E51031 CRC64;
     MPGDPTATAK GNEIPDTLMG YIPWTPELDS GEVCGIPTTF KTRDEWKGKK VVIVSIPGAY
     TPICHQQHIP PLVKRVDELK AKGVDAVYVI ASNDPFVMAA WGNFNNAKDK VVFATDIDLA
     FSKALGATID LSAKHFGERT ARYALIIDDN KIVDFASDEG DTGKLQNASI DTILTKV
//