ID   TRXB_PEPAC              Reviewed;         315 AA.
AC   P50971;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-FEB-2025, entry version 109.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB;
OS   Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC   Peptoclostridiaceae; Peptoclostridium.
OX   NCBI_TaxID=1731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX   PubMed=8223622; DOI=10.1111/j.1432-1033.1993.tb18307.x;
RA   Luebbers M., Andreesen J.R.;
RT   "Components of glycine reductase from Eubacterium acidaminophilum. Cloning,
RT   sequencing and identification of the genes for thioredoxin reductase,
RT   thioredoxin and selenoprotein PA.";
RL   Eur. J. Biochem. 217:791-798(1993).
RN   [2]
RP   SEQUENCE REVISION TO 275.
RA   Andreesen J.R.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-54.
RX   PubMed=2537814; DOI=10.1128/jb.171.3.1346-1354.1989;
RA   Freundenberg W., Dietrichs D., Lebertz H., Andreesen J.R.;
RT   "Isolation of an atypically small lipoamide dehydrogenase involved in the
RT   glycine decarboxylase complex from Eubacterium acidaminophilum.";
RL   J. Bacteriol. 171:1346-1354(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         NADPH + H(+); 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; L04500; AAB93303.1; -; Genomic_DNA.
DR   PIR; S38988; D35156.
DR   AlphaFoldDB; P50971; -.
DR   SMR; P50971; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
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   InterPro; IPR050097; Ferredoxin-NADP_redctase_2.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   NCBIfam; TIGR01292; TRX_reduct; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 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.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   NADP; Oxidoreductase; Redox-active center.
FT   CHAIN           1..315
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166731"
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;  34034 MW;  145B0EABB2B8A7FA CRC64;
     MENVYDLAII GSGPAGLAAA LYGARAKMKT IMIEGQKVGG QIVITHEVAN YPGSVREATG
     PSLIERMEEQ ANEFGAEKVM DKIVDVDLDG KIKVIKGEKA EYKAKSVILA TGAAPRLAGC
     PGEQELTGKG VSYCATCDAD FFEDMEVFVV GGGDTAVEEA MYLAKFARKV TIVHRRDELR
     AAKSIQEKAF KNPKLDFMWN SAIEEIKGDG IVESAVFKNL VTGETTEYFA NEEDGTFGIF
     VFIGYIPKSD VFKGKITLDD AGYIITDDNM KTNVEGVFAA GDIRVKSLRQ VVTACADGAI
     AATQAEKYVE ANFEE
//