ID   Q6FMP9_CANGA            Unreviewed;       198 AA.
AC   Q6FMP9;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN   Name=TSA1 {ECO:0000313|CGD:CAL0134717};
GN   OrderedLocusNames=CAGL0K06259g {ECO:0000313|CGD:CAL0134717,
GN   ECO:0000313|EMBL:CAG61456.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG61456.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG61456.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380957; CAG61456.1; -; Genomic_DNA.
DR   RefSeq; XP_448495.1; XM_448495.1.
DR   AlphaFoldDB; Q6FMP9; -.
DR   STRING; 284593.Q6FMP9; -.
DR   PeroxiBase; 4469; Cgl2CysPrx02.
DR   EnsemblFungi; CAGL0K06259g-T; CAGL0K06259g-T-p1; CAGL0K06259g.
DR   GeneID; 2890460; -.
DR   KEGG; cgr:CAGL0K06259g; -.
DR   CGD; CAL0134717; TSA1.
DR   VEuPathDB; FungiDB:CAGL0K06259g; -.
DR   eggNOG; KOG0852; Eukaryota.
DR   HOGENOM; CLU_042529_21_0_1; -.
DR   InParanoid; Q6FMP9; -.
DR   OMA; FWYPKDF; -.
DR   PHI-base; PHI:9714; -.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:RHEA.
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; AT16346P-RELATED; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
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:UP000002428};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..161
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        48
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   198 AA;  21868 MW;  31707FBCD96379BB CRC64;
     MVAQVQKPAP TFKKTAVIDG MFEEVSLDKY KGKYVVLAFV PLAFTFVCPT EIVAFSEAAK
     RFEALDAQVL FASTDSEYSL LAWTNVARKD GGLGPVDIPL LADTNHKLSR DYGVLIEDEG
     IALRGLFIID PKGIVRHITI NDLPVGRNVE ESLRLVEGFQ WTDKNGTVLP CNWTPGSATI
     KPTVEDSKEY FKEANSKN
//