ID A0A1E5GRL0_9ENTE Unreviewed; 562 AA.
AC A0A1E5GRL0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:OEG14860.1};
GN ORFNames=BCR23_12265 {ECO:0000313|EMBL:OEG14860.1};
OS Enterococcus quebecensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=903983 {ECO:0000313|EMBL:OEG14860.1, ECO:0000313|Proteomes:UP000094764};
RN [1] {ECO:0000313|EMBL:OEG14860.1, ECO:0000313|Proteomes:UP000094764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26306 {ECO:0000313|EMBL:OEG14860.1,
RC ECO:0000313|Proteomes:UP000094764};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:OEG14860.1}.
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DR EMBL; MIKB01000018; OEG14860.1; -; Genomic_DNA.
DR RefSeq; WP_069636090.1; NZ_MIKB01000018.1.
DR AlphaFoldDB; A0A1E5GRL0; -.
DR STRING; 903983.BCR23_12265; -.
DR PATRIC; fig|903983.4.peg.558; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000094764; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03026; AhpF_NTD_C; 1.
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; IPR044141; AhpF_NTD_C.
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.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 6..296
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 485..560
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT REGION 328..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 562 AA; 61330 MW; AC146C5858BC9126 CRC64;
MSQEIYDLIV IGGGSAALSA GIYAGRAMLD TLIIEKDKIG GQVTTTSEIV NYPAIRATTG
PELMEDMRLQ ALDFGVEFTT DEIIDVDLSQ TVKTVKSATK TYQAYAVIIA TGASARKIGF
PGEVEFTGRG IAYCSTCDGE FFQGLDIFVL GGGYAAAEEA VYLTRYGKSV TMIIREPDFT
CAKLTAEAAK QHPDIKIVYN TEVKEITGDD FVRKAVFVNN ETGEETTYDA PEGSTFGMFV
FAGNKPSTEI FEGKVELDRG YVPTNENMET NVPGVYAAGD LRIKELRQIV TAVADGAIAA
TNAQKYITEE KTKAGLPIVN ERMEKRLAEQ HAASKKEQPK TEKKAVKATS GNNTWFPDAM
REQLGGIFGK LTKNVTLLQV MDSSEEKSLE LNSFLTEFAS LSDKILLESI QKGEKPDLET
KYGIDKLPSV VVLNDQGDYT GIKFSGIPSG HEVNSIVLAV YNVGSAGQPI EEPVVNKIKE
LPKKKVQIFV SLTCHYCPDV VAACQRIASI NHNVEAEMID IGVFPELKTE KKIMSVPAMI
IDDKEIVFGS KNMDEIVEIL EK
//
