ID   A0A175WK63_9PEZI        Unreviewed;       313 AA.
AC   A0A175WK63;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:KXX83234.1};
GN   ORFNames=MMYC01_200286 {ECO:0000313|EMBL:KXX83234.1};
OS   Madurella mycetomatis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX   NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX83234.1, ECO:0000313|Proteomes:UP000078237};
RN   [1] {ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   van de Sande W.W.J.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXX83234.1, ECO:0000313|Proteomes:UP000078237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA   Van De Sande W.;
RT   "Madurella mycetomatis genome sequencing.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:KXX83234.1}.
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DR   EMBL; LCTW02000002; KXX83234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A175WK63; -.
DR   STRING; 100816.A0A175WK63; -.
DR   VEuPathDB; FungiDB:MMYC01_200286; -.
DR   OrthoDB; 1447958at2759; -.
DR   Proteomes; UP000078237; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097237; P:cellular response to toxic substance; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078237}.
FT   DOMAIN          6..296
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   313 AA;  33512 MW;  EA51354AE4077633 CRC64;
     MPALLDVLII GGGPAGLSVA TGLARQLYTA VVFDSGVYRN ARTKHMHNVP TWDHRDPADF
     RAAARRDILA RYNTIQFQEA KIETVRRTED GRFEATDAKG TTWLGKKLVL ASGMKDVYPD
     IPGYDDVWGR GVYHCLFCDG FEDRGSASAG VLAVGDIAKP PPALHLSRMA KRLAKKVVVY
     TNGASELSEQ IAAALGNDPV ITLDNRRVTR LEKVKDGSSE TIVHLEDGTK VSHGFVVHKP
     KNEINGPFAK QLGVELNEMG VIKTTQPFYE TTVPGVFAAG DCAAPMPAVS NALAMGAFVA
     GGLVAQLGAE PTA
//