ID A0A165FEV8_XYLHT Unreviewed; 167 AA.
AC A0A165FEV8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Redoxin {ECO:0000313|EMBL:KZF20896.1};
GN ORFNames=L228DRAFT_249728 {ECO:0000313|EMBL:KZF20896.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF20896.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF20896.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF20896.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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}.
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DR EMBL; KV407462; KZF20896.1; -; Genomic_DNA.
DR RefSeq; XP_018186451.1; XM_018333152.1.
DR AlphaFoldDB; A0A165FEV8; -.
DR STRING; 1328760.A0A165FEV8; -.
DR GeneID; 28898289; -.
DR InParanoid; A0A165FEV8; -.
DR OMA; YNASKEF; -.
DR OrthoDB; 593245at2759; -.
DR Proteomes; UP000076632; 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:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 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:UP000076632}.
FT DOMAIN 4..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 61
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 167 AA; 17892 MW; 06E2626366456C39 CRC64;
MSGLKVGEQF PQDVVFSYVP YTEEKSDITA CGIPQNYNAS KEFAGKKVVL FSVPGAFTPG
CSARHLPGYI EHLKDFKSKG VDIVAVIAFN DAWVMSAWGK ANGIKGDDIL FLSDPDAKFS
SSIGWTAGPR TARYALALDN NKVIYAEKEP APGEVTVSGA EAVLAKL
//
