ID   A0A419T263_9FIRM        Unreviewed;       545 AA.
AC   A0A419T263;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:RKD31519.1};
GN   ORFNames=BET01_20430 {ECO:0000313|EMBL:RKD31519.1};
OS   Lacrimispora algidixylanolytica.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lacrimispora.
OX   NCBI_TaxID=94868 {ECO:0000313|EMBL:RKD31519.1, ECO:0000313|Proteomes:UP000284277};
RN   [1] {ECO:0000313|EMBL:RKD31519.1, ECO:0000313|Proteomes:UP000284277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPL73 {ECO:0000313|EMBL:RKD31519.1,
RC   ECO:0000313|Proteomes:UP000284277};
RA   Poppleton D.I., Gribaldo S.;
RT   "A new outlook on sporulation: Clostridium algidixylanolyticum.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:RKD31519.1}.
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DR   EMBL; MCIA01000018; RKD31519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A419T263; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000284277; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.80; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017561; AhpF_homologue_put.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR03143; AhpF_homolog; 1.
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   Pfam; PF13192; Thioredoxin_3; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284277}.
FT   DOMAIN          5..296
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          467..542
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
SQ   SEQUENCE   545 AA;  59874 MW;  B1F0C1E57AA62F0E CRC64;
     MDGLYDVIVV GTGPAGLSAA IYAARARFKV LVLEKEKLGG QITITSEVVN YPGIESIDGT
     TLTDKMRKQA ENFGAEFKMA KVLDMDLSQE LRVVKTDKGD LKALGVVLAL GANPRMIGFQ
     GEETFKGRGV AYCATCDGEF FTGMDVFVIG GGYAAAEEAV FLTKYAKKVT IIVREDDFTC
     AGSVADKARE HEKIEVHYHT EIVEAAGDTL LRTAKFRDIK TGEEWQYDTP EGETFGIFVF
     AGYVPDTSWI HGKVALNHDG YIITDPDQMT DIPGIYGAGD VCVKNLRQVV TAVSDGAIAA
     TSLEKYVADM WEKLGIEKRE EPVKAEYKAD GHSEESVEGD EFITPEMKLQ LKDLFGKFER
     KVTVKALLNK SPLAAQMEGF LKELSGISDQ VECLVSWESE ETTTDEKLPA ICVLKEDGTE
     SGLRFYAIPG GHEFNSFVIG LYNVAGPGQA ISPEEAQRIK EIKKPVDIIV AVSLSCTMCP
     TTVMSAGRIA AENELVNAWT YDLNLYPELK ERYQIMSVPC MIINQKKVEF GKKSLEDLLN
     ILETI
//