ID A0A1H0SS14_HALAD Unreviewed; 324 AA.
AC A0A1H0SS14;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Thioredoxin reductase (NADPH) {ECO:0000313|EMBL:SDP44494.1};
GN ORFNames=SAMN05421677_1193 {ECO:0000313|EMBL:SDP44494.1};
OS Halobacillus aidingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=240303 {ECO:0000313|EMBL:SDP44494.1, ECO:0000313|Proteomes:UP000198860};
RN [1] {ECO:0000313|EMBL:SDP44494.1, ECO:0000313|Proteomes:UP000198860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3703 {ECO:0000313|EMBL:SDP44494.1,
RC ECO:0000313|Proteomes:UP000198860};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FNIZ01000019; SDP44494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0SS14; -.
DR STRING; 240303.SAMN05421677_1193; -.
DR OrthoDB; 9778740at2; -.
DR Proteomes; UP000198860; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR023856; Bdr.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR NCBIfam; TIGR04018; Bthiol_YpdA; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF13738; Pyr_redox_3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 324 AA; 36433 MW; 42D2237BE5BFD37B CRC64;
MQEEKVIIIG GGPCGMSAAI ELQKEGIEPL IIEKGNIVNS IYHYPTHQTF FSSSEKLEIG
NIPFITERQK PVRNEALAYY RAVAGREDLR VNTYEKVTQV DRNDHGFIIQ SQTGDGEGKS
YRANQIVIAT GYYDQPNYMN VKGEDLPKVK HYFKEGHPYY KKKVVIIGGK NSAADAALEL
EKSGALITVL YRGEDYSKSI KPWILPQFEA LVKKGIIDME FCANVKEITE DEVVYECHGQ
EKRIENDFVF AMTGYRPDHA FLTKMGVEMD EETGRPAFDE DTMETNVEGI YIAGVIAAGY
NNNEIFIENG RHHGGKIAKA VTNK
//