ID   TRXB_PEPLI              Reviewed;         315 AA.
AC   P52213;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB;
OS   Peptoclostridium litorale (Clostridium litorale).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptoclostridium.
OX   NCBI_TaxID=1557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8529640; DOI=10.1111/j.1432-1033.1995.192_c.x;
RA   Kreimer S., Andreesen J.R.;
RT   "Glycine reductase of Clostridium litorale. Cloning, sequencing, and
RT   molecular analysis of the grdAB operon that contains two in-frame TGA
RT   codons for selenium incorporation.";
RL   Eur. J. Biochem. 234:192-199(1995).
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:P0A9P4};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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}.
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DR   EMBL; U24268; AAC43575.1; -; Genomic_DNA.
DR   PIR; S63990; S63990.
DR   AlphaFoldDB; P52213; -.
DR   SMR; P52213; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
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.
FT   CHAIN           1..315
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166727"
FT   BINDING         34..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         282..291
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   DISULFID        134..137
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   315 AA;  33946 MW;  2CA55D36E579E2EF CRC64;
     MENVYDIAII GSGPAGLAAA LYGARAKMKT LLLEGMKVGG QIVITHEVAN YPGSVPEATG
     PSLIGRMEEQ VEEFGAERVM DNIVDVDFTD KIKVLKGAKG EYKAKAVIVA TGASPKLAGC
     PGEKELTGKG VSYCATCDAD FFEDMEVFVI GGGDTAVEEA MFLTKFARKV TIVHRRAELR
     AAKSIQEKAF KNEKLNFMWN TVIEEIKGDG IVESAVFKNR ETGEVTEFVA PEEDGTFGIF
     VFIGYDPKSA LVEGKLELDE TGYIPTDDNM KTNVEGVFAA GDIRVKSLRQ VVTATADGAI
     AAVQAEKYIE ELFAE