ID   R9N1G9_9FIRM            Unreviewed;       332 AA.
AC   R9N1G9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Thioredoxin-disulfide reductase {ECO:0000313|EMBL:EOS77164.1};
GN   ORFNames=C819_01190 {ECO:0000313|EMBL:EOS77164.1};
OS   Lachnospiraceae bacterium 10-1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1235800 {ECO:0000313|EMBL:EOS77164.1, ECO:0000313|Proteomes:UP000014134};
RN   [1] {ECO:0000313|EMBL:EOS77164.1, ECO:0000313|Proteomes:UP000014134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-1 {ECO:0000313|EMBL:EOS77164.1,
RC   ECO:0000313|Proteomes:UP000014134};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 10-01.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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:EOS77164.1}.
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DR   EMBL; ASTF01000010; EOS77164.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9N1G9; -.
DR   STRING; 1235800.C819_01190; -.
DR   PATRIC; fig|1235800.3.peg.1279; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_3_9; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000014134; Unassembled WGS sequence.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
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; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014134}.
FT   DOMAIN          2..317
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   COILED          76..106
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   332 AA;  35335 MW;  73C3EF2F400488BB CRC64;
     MYDLVIIGSG PAGLSASIYA KRAGLNAVTL EQNPMSGGQV LNTYEVDNYP GLPGINGFDL
     GMKFREHADK LGCEFMEAAV QEIKTVEAAR REANQKEEGK AEMKAASLPE NRKMDSGFIV
     ATDQEEIKTR TILAAMGATH AKLGVPGEEE LTGMGVSYCA TCDGAFFRGK VTAVVGGGDV
     AVEDAIFLAR ACEKVYLIHR RDELRAAAVL QKEVMSLPNV EILWDTVAKK IEGSDKVQAL
     VLENVKTGEN KVLAVDGVFV AVGIIPSGDI LKGLVKQDEN GYVLAGEDCM TSMSGVFAAG
     DIRKKKLRQV VTAVADGANA VTSVLEYLNG VK
//