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Database: UniProt
Entry: A0A0C9M814_9FUNG
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ID   A0A0C9M814_9FUNG        Unreviewed;       198 AA.
AC   A0A0C9M814;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN   ORFNames=MAM1_0035c02650 {ECO:0000313|EMBL:GAN03199.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN03199.1};
RN   [1] {ECO:0000313|EMBL:GAN03199.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN03199.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. {ECO:0000256|PIRNR:PIRNR000239}.
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:0000256|ARBA:ARBA00000280};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009796}.
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DR   EMBL; DF836324; GAN03199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9M814; -.
DR   STRING; 91626.A0A0C9M814; -.
DR   OrthoDB; 47465at2759; -.
DR   Proteomes; UP000053815; Unassembled WGS sequence.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF171; PEROXIREDOXIN-4; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|PIRNR:PIRNR000239};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000239}; Peroxidase {ECO:0000256|PIRNR:PIRNR000239};
KW   Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT   DOMAIN          4..163
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        50
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   198 AA;  22196 MW;  30CFEEEF73B0DFFB CRC64;
     MVVAQVQKPA PEFDAPGVID GQIVEHIKLS DYRGKYVVLF WYPMDFTFVC PTEIIAFNDA
     YEEFQSLDCQ LIAASCDSEY AHHAWINLPR ESGGLGEQTK IPIISDKTKA IAKSYGVYLE
     QGISLRGLFI IDPKGIVRQI TINDLSVGRS TTETIRLVEA FQFTDKHGEV CPANWNKGSK
     TIIPDVEKAK AYFQDDDD
//
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