ID M3JZD9_CANMX Unreviewed; 184 AA.
AC M3JZD9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN ORFNames=G210_1743 {ECO:0000313|EMBL:EMG47809.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG47809.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG47809.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000256|RuleBase:RU366011}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010505, ECO:0000256|RuleBase:RU366011}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG47809.1}.
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DR EMBL; AOGT01001366; EMG47809.1; -; Genomic_DNA.
DR AlphaFoldDB; M3JZD9; -.
DR STRING; 1245528.M3JZD9; -.
DR eggNOG; KOG0541; Eukaryota.
DR HOGENOM; CLU_072440_3_0_1; -.
DR OMA; PTCHSAH; -.
DR OrthoDB; 593245at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF39; PEROXIREDOXIN AHP1; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|RuleBase:RU366011};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366011};
KW Peroxidase {ECO:0000256|RuleBase:RU366011};
KW Redox-active center {ECO:0000256|RuleBase:RU366011};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT DOMAIN 25..184
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 69
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 184 AA; 20156 MW; 5BDFDCDC335074C3 CRC64;
MFSLAKSFPK VQLTQSIRNS LRTYVAVGDK IPSTTVFEGA PNNEVNLADE TASGKSIIIG
VPGAFSTACS ATHVPAYIRR IRAFNDKNFH KLFIVSVNDA FVTKAWGDQL LDSVAGEQIR
FIADPKGDFT KELDLLFDAS KFFGNERSKR YALIVEDGQV VKSFVEPDNT SVNVSSAENV
LEEA
//
