ID   D8GNH2_CLOLD            Unreviewed;       315 AA.
AC   D8GNH2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE            EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN   Name=trxB_2 {ECO:0000313|EMBL:OAA84295.1};
GN   ORFNames=WX45_01152 {ECO:0000313|EMBL:OAA84295.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:OAA84295.1, ECO:0000313|Proteomes:UP000077020};
RN   [1] {ECO:0000313|EMBL:OAA84295.1, ECO:0000313|Proteomes:UP000077020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PETC {ECO:0000313|EMBL:OAA84295.1,
RC   ECO:0000313|Proteomes:UP000077020};
RX   PubMed=26331212; DOI=10.1002/bit.25827;
RA   Martin M.E., Richter H., Saha S., Angenent L.T.;
RT   "Traits of selected Clostridium strains for syngas fermentation to
RT   ethanol.";
RL   Biotechnol. Bioeng. 113:531-539(2016).
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         Evidence={ECO:0000256|RuleBase:RU003880};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003881};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333,
CC       ECO:0000256|RuleBase:RU003880}.
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:OAA84295.1}.
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DR   EMBL; LITS01000025; OAA84295.1; -; Genomic_DNA.
DR   RefSeq; WP_013239425.1; NC_014328.1.
DR   AlphaFoldDB; D8GNH2; -.
DR   KEGG; clj:CLJU_c27810; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000077020; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003880};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003880}; NADP {ECO:0000256|RuleBase:RU003881};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003880};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003880};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077020}.
FT   DOMAIN          5..298
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   315 AA;  34355 MW;  89C718C33D247181 CRC64;
     MNNIYDVIII GSGPAGLSAA LYSARAKMKT LLLERSKAGG QIVITDEVAN YPGSIKEATG
     PSLIARMEEQ VESFGAERKK DEIKEVDFTG KIKRLKGIKE EYQAKAVIIA TGATPRHIGC
     PGENQLIGKG VSYCATCDAE FFEDLEVFVV GGGDAAIEEA LYLTKFAKKV TIVHRRDELR
     AAKSIQEKAF KNPKVEIMWN KVITELKGDG LLESAVFKDT KTGEINEYFA DEEDGTFGVF
     VFVGYLPING LFKDKITMNK AGYIITNDKM ETNISGVFAA GDIREKPLRQ VVTAAADGAI
     AAVEAGKYIE NNFEE
//