ID   PMP20_LIPKO             Reviewed;         166 AA.
AC   Q01116;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Putative peroxisomal peroxiredoxin;
DE            EC=1.11.1.-;
OS   Lipomyces kononenkoae (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=34357;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 44833 / BCRC 21537 / CBS 5608 / IGC 4052 / JCM 5990 / NBRC
RC   10376 / NRRL Y-11554;
RX   PubMed=7958767; DOI=10.1111/j.1574-6968.1994.tb07158.x;
RA   Randez-Gil F., Prieto J., Sanz P.;
RT   "Nucleotide sequence of a putative peroxisomal protein from the yeast
RT   Lipomyces kononenkoae.";
RL   FEMS Microbiol. Lett. 122:153-157(1994).
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=[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an
CC         alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation.
CC       {ECO:0000250|UniProtKB:P38013}.
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; U11244; AAB41351.1; -; mRNA.
DR   AlphaFoldDB; Q01116; -.
DR   SMR; Q01116; -.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:RHEA.
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   2: Evidence at transcript level;
KW   Antioxidant; Disulfide bond; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN           1..166
FT                   /note="Putative peroxisomal peroxiredoxin"
FT                   /id="PRO_0000056608"
FT   DOMAIN          5..166
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        56
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P38013"
FT   DISULFID        26
FT                   /note="Interchain (with C-56); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P38013"
FT   DISULFID        56
FT                   /note="Interchain (with C-26); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P38013"
SQ   SEQUENCE   166 AA;  17408 MW;  72BBC556F979E0E3 CRC64;
     MTDKFPEDVK FLYIAYTPAK ADITACGIPI PLDFDKEFRD KTVVIVAIPG AFTPTCTANH
     IPPFVEKFTA LKSAGVDAVI VLSANDPFVQ SAFGKALGVT DEAFIFASDP GAEFSKSAGL
     SLDLPPAFGT RTARYAIIVS NGVVKYVEKD SEGVAGSGVD AVLAAL