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Database: UniProt
Entry: A0A448YHQ5_BRENA
LinkDB: A0A448YHQ5_BRENA
Original site: A0A448YHQ5_BRENA 
ID   A0A448YHQ5_BRENA        Unreviewed;       247 AA.
AC   A0A448YHQ5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=DEKNAAC101302 {ECO:0000313|EMBL:VEU20408.1};
GN   ORFNames=BRENAR_LOCUS1143 {ECO:0000313|EMBL:VEU20408.1};
OS   Brettanomyces naardenensis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=13370 {ECO:0000313|EMBL:VEU20408.1, ECO:0000313|Proteomes:UP000290900};
RN   [1] {ECO:0000313|EMBL:VEU20408.1, ECO:0000313|Proteomes:UP000290900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tiukova I., Dainat J.;
RL   Submitted (DEC-2018) 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   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC       {ECO:0000256|ARBA:ARBA00025719}.
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DR   EMBL; CAACVR010000004; VEU20408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A448YHQ5; -.
DR   STRING; 13370.A0A448YHQ5; -.
DR   InParanoid; A0A448YHQ5; -.
DR   Proteomes; UP000290900; Unassembled WGS sequence.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR   CDD; cd03016; PRX_1cys; 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; IPR045020; PRX_1cys.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR   PANTHER; PTHR43503:SF9; PEROXIREDOXIN PRX1, MITOCHONDRIAL; 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|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000239};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239};
KW   Redox-active center {ECO:0000256|PIRNR:PIRNR000239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290900}.
FT   DOMAIN          31..195
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        73
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   247 AA;  27439 MW;  8B11B4C1BFFA5240 CRC64;
     MFARSFFRIP SKSLAASVRF LTFDAAKQPR VRIGSTAPNF QAPSTVGEID LYKYLGNSWG
     VLFSHPADFT PVCTTELGEF AALKPEFDAR GVKLLGLSAD ELGKHEQWVE DIKDISLGGK
     KFNYPIISDS KKEVAFLYDM VSEDAFNKIN EGPIATVRSV FIIDPKKKVR LVITYPPSVG
     RNTSEVLRVI DSLQVGDKLG VVTPVNWKKG EDVIIPPTVS NEAAKEKFGD FKTVKPYLRY
     TSPETKN
//
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