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Database: UniProt
Entry: A0A1M4YFD7_9CLOT
LinkDB: A0A1M4YFD7_9CLOT
Original site: A0A1M4YFD7_9CLOT 
ID   A0A1M4YFD7_9CLOT        Unreviewed;       551 AA.
AC   A0A1M4YFD7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Thioredoxin reductase (NADPH) {ECO:0000313|EMBL:SHF04222.1};
GN   ORFNames=SAMN02745158_02344 {ECO:0000313|EMBL:SHF04222.1};
OS   Lactonifactor longoviformis DSM 17459.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Lactonifactor.
OX   NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHF04222.1, ECO:0000313|Proteomes:UP000184245};
RN   [1] {ECO:0000313|EMBL:SHF04222.1, ECO:0000313|Proteomes:UP000184245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17459 {ECO:0000313|EMBL:SHF04222.1,
RC   ECO:0000313|Proteomes:UP000184245};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQVI01000011; SHF04222.1; -; Genomic_DNA.
DR   RefSeq; WP_072851921.1; NZ_FQVI01000011.1.
DR   AlphaFoldDB; A0A1M4YFD7; -.
DR   STRING; 1122155.SAMN02745158_02344; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000184245; 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.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184245}.
FT   DOMAIN          6..298
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          470..543
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
SQ   SEQUENCE   551 AA;  60750 MW;  77B4C8D959C7BBED CRC64;
     MEHGIYDLLI LGGGCAGLTA GIYAGRAKLK AAVVEKQGAG GQAAITDEIA NYPGFRKISG
     TELAERMLEQ ASSFGTEFLQ QDVVNLKLTQ EIKEVETSSG VLKSRAVILA TGAEPKKLGF
     QGEEEFRGRG IGYCATCDGF FFEGKDIFVI GGGYSAAEEA LYLTRFGKKV TVVVRKGAFK
     CAKSISDKVL SHPKIEVMFH TEITEAYGDT VLRGAVFKNN QTGETFEYKV SEEDETFGIF
     VFIGYQPSTE LYRGQVTLDE AGHVITNERM ETNLSGVYAA GDLRPKLLRQ LVTATADGAI
     AATQVEKYIT EYKEKHGIRE EKNLNVSEQT EADSVDGPAI ISQDLRSQVQ TVFDKLERET
     YLAVILDDSR KSEELKKFCE EVCSICKRIH MVIRRKGEDK ELEAEVNAEN YPMIALLKET
     KEYSGVKFSG IPAGHEFNSF VLAVYNLSGP GQGVEESVQN RVMAVKRRVK LQIAISLSCH
     FCPETVIAAQ HLAILNPQIE AEMIDISMFP QLKKTYSLMS VPALIINEKQ TVFGALSMEQ
     ILEQIEKVGQ L
//
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