ID A0A1Y3XYR2_9FIRM Unreviewed; 550 AA.
AC A0A1Y3XYR2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:OUN90686.1};
GN ORFNames=B5G00_15390 {ECO:0000313|EMBL:OUN90686.1};
OS Blautia sp. An46.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1965636 {ECO:0000313|EMBL:OUN90686.1, ECO:0000313|Proteomes:UP000196301};
RN [1] {ECO:0000313|Proteomes:UP000196301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An46 {ECO:0000313|Proteomes:UP000196301};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUN90686.1}.
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DR EMBL; NFIF01000021; OUN90686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3XYR2; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000196301; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02974; AhpF_NTD_N; 1.
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; IPR044142; AhpF_NTD_N.
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:UP000196301}.
FT DOMAIN 7..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 468..533
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
SQ SEQUENCE 550 AA; 60154 MW; 20E3873793449A5B CRC64;
MADKFYDGVI IGGGPAGLAA AIYLARARYR VLVIEKETIG GQITITSEVV NYPGVLHTDG
KKLTEEMRKQ AQNFGAEFLK AQVTSLALEG DKKKILTDKG EIQALGVVLA TGASPRQAGF
KGEEEFRGRG VAYCATCDGE FFTGKDIFVV GGGFAAVEEA LFLTRYARKI RVVVRGKEIN
CAGPAVEELL AHPDISVSFE TEITEAGGKD MLEYVVLRKK DTGEIFTVQA EEGENLGIFV
FAGYVPATEL FRDQVKVSDK GYLLANRKQE TNVPGVYGAG DVCEKELRQV VTAVSDGAVA
AASMEKYLFS IYQKLGIKRE KRKITEVKKP AQGEEKEKIS SGGEGFLTEE MKESLVPVFA
RFEKEILVKV YLDASYLSRE VEGFVREMEP LSEKVRYEIQ RAGAEGVTCP SLRICDSQGN
YLGAEFHGVP GGHEFNSFII ALYNGAGPGQ SMGEDIRRRI QNITGKTDLK IAVSLSCTMC
PDVVMAAQKI ALENPLVTAE MFDLAHYPEL KEKYQIMSVP CLILNDSRVS FGKKGIGQIL
DLLEETAEEI
//
