ID   TRXR_ARTBC              Reviewed;         404 AA.
AC   D4APQ6;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Probable thioredoxin reductase ARB_06224 {ECO:0000305};
DE            EC=1.8.1.9 {ECO:0000250|UniProtKB:P0A9P4};
DE   Flags: Precursor;
GN   ORFNames=ARB_06224;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21919205; DOI=10.1002/pmic.201100234;
RA   Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA   Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT   "Identification of novel secreted proteases during extracellular
RT   proteolysis by dermatophytes at acidic pH.";
RL   Proteomics 11:4422-4433(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P0A9P4};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P0A9P4};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; ABSU01000004; EFE35267.1; -; Genomic_DNA.
DR   RefSeq; XP_003015912.1; XM_003015866.1.
DR   AlphaFoldDB; D4APQ6; -.
DR   SMR; D4APQ6; -.
DR   STRING; 663331.D4APQ6; -.
DR   EnsemblFungi; EFE35267; EFE35267; ARB_06224.
DR   GeneID; 9523739; -.
DR   KEGG; abe:ARB_06224; -.
DR   eggNOG; ENOG502S4MV; Eukaryota.
DR   HOGENOM; CLU_031864_5_0_1; -.
DR   OMA; AAIWIHK; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..404
FT                   /note="Probable thioredoxin reductase ARB_06224"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434676"
FT   BINDING         67..75
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         334..343
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        172..175
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   404 AA;  45299 MW;  58850D1A2BBD7041 CRC64;
     MGVQRLALAL IAFTSALTSV IAAPIVIEQP PLGPEHRYDA IVIGGGPSGL SALSSLGRVR
     RHVLLFDEGI YRNGATRHIH DMLTNDGVEP KVFRAKARQQ ISRYTSTSIK DVKVTKIKKV
     FEHGGRKYFF QVTDKTGAMY TASKVVLGTG VLDVLPGTPG LQENFGKGIY WCPWCDGWEH
     RDQPLGILGP LRHVMDSVYE LETLNNDIIA FVNGTEHSVE DILYLNRKYP HWRQQLKHYN
     VQINNKMVSS IDRLQDGSKH QDKKTWQEFD KFRVNFNDGT SVERSVFITN FPTEQHSDLP
     DQLGLARDPI HKNKIKVNFK GMRASVPGVF VVGDANNDGS TNGNHAMFSG KRAAVALHVE
     LEQERAEAAL GKRDESFSAE QVENEALKLI GRDTEELEEL WGRK