ID   TRXB_ASHGO              Reviewed;         319 AA.
AC   Q75CM8;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Thioredoxin reductase;
DE            EC=1.8.1.9;
GN   Name=TRR1; OrderedLocusNames=ACL109C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P29509};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P29509};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29509}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29509}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS51119.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016816; AAS51119.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_983295.1; NM_208648.1.
DR   AlphaFoldDB; Q75CM8; -.
DR   SMR; Q75CM8; -.
DR   STRING; 33169.AAS51119; -.
DR   GeneID; 4619415; -.
DR   KEGG; ago:AGOS_ACL109C; -.
DR   eggNOG; KOG0404; Eukaryota.
DR   InParanoid; Q75CM8; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..319
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166761"
FT   BINDING         11..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         40..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         145
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         288
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   BINDING         295..297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
FT   DISULFID        142..145
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P29509"
SQ   SEQUENCE   319 AA;  34117 MW;  F7151B685B7802FC CRC64;
     MVHHKVTIIG SGPAAHTAAI YLARAEIKPT LYEGMFANGV AAGGQLTTTT EIENFPGFPD
     GLTGSDLMER MKAQSVKFGT EVVTETVAKV DLSARPFKLW TEFNEDEEPT TTDAIILATG
     ASAKRLGLPG EETYWQRGIS ACAVCDGAVP IFRNKPLAVV GGGDSACEEA SFLTKYGSKV
     FMLVRKDHMR ASTIMQRRVE RNEKIEVLYN TAPVEAKGDG SLLDALRVRD TRTGEESDLP
     VNGLFYAIGH TPATQLVAGQ VDLDESGYVK TVPGSTLTNV PGLFAAGDVQ DSRYRQAVTS
     AGSGCMAALD AEKFLSELE