ID   PMPB_CANBO              Reviewed;         167 AA.
AC   P14293;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Putative peroxiredoxin-B;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P38013};
DE   AltName: Full=PMP20;
DE   AltName: Full=Peroxisomal membrane protein B;
DE   AltName: Full=Thioredoxin reductase;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin-B {ECO:0000305};
DE   AltName: Allergen=Cand b 2;
GN   Name=PMPB;
OS   Candida boidinii (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX   NCBI_TaxID=5477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, SUBCELLULAR
RP   LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 32195;
RX   PubMed=2760051; DOI=10.1016/s0021-9258(18)80089-8;
RA   Garrard L.J., Goodman J.M.;
RT   "Two genes encode the major membrane-associated protein of methanol-induced
RT   peroxisomes from Candida boidinii.";
RL   J. Biol. Chem. 264:13929-13937(1989).
RN   [2]
RP   CROSS-REACTIVITY WITH ASP F 3.
RX   PubMed=9412580; DOI=10.1164/ajrccm.156.6.9702087;
RA   Hemmann S., Blaser K., Crameri R.;
RT   "Allergens of Aspergillus fumigatus and Candida boidinii share IgE-binding
RT   epitopes.";
RL   Am. J. Respir. Crit. Care Med. 156:1956-1962(1997).
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=[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:P38013};
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein
CC       {ECO:0000269|PubMed:2760051}.
CC   -!- INDUCTION: By methanol. {ECO:0000269|PubMed:2760051}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Shares common IgE-
CC       binding epitopes with allergen Asp f 3 of Aspergillus fumigatus.
CC       {ECO:0000269|PubMed:9412580}.
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 1-Cys
CC       peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC       with a cysteine from another protein or with a small thiol molecule.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; J04985; AAA34358.1; -; Genomic_DNA.
DR   PIR; B32646; B32646.
DR   AlphaFoldDB; P14293; -.
DR   SMR; P14293; -.
DR   Allergome; 178; Cand b 2.
DR   Allergome; 3175; Cand b 2.0101.
DR   OrthoDB; 1281610at2759; -.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
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; Membrane;
KW   Methanol utilization; Oxidoreductase; Peroxidase; Peroxisome;
KW   Redox-active center.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2760051"
FT   CHAIN           2..167
FT                   /note="Putative peroxiredoxin-B"
FT                   /id="PRO_0000056605"
FT   DOMAIN          4..167
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           165..167
FT                   /note="Microbody targeting signal"
FT   ACT_SITE        53
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P38013"
SQ   SEQUENCE   167 AA;  18056 MW;  A3909D7C6ACFBFD0 CRC64;
     MAPIKRGDRF PTTDDVYYIP PEGGEPGAFE LSKFVKTKKF VVVSVPGAFT PPCTEQHLPG
     YIKNLPRILS KGVDFVLVIT QNDPFVLKGW KKELGAADAK KLIFVSDPNL KLTKKLGSTI
     DLSSIGLGTR SGRLALIVNR SGIVEYAAIE NGGEVDVSTA QKIIAKL