ID   A0A1K2FKX3_9ACTN        Unreviewed;       311 AA.
AC   A0A1K2FKX3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Thioredoxin reductase {ECO:0000313|EMBL:SFY47687.1};
DE            EC=1.8.1.9 {ECO:0000313|EMBL:SFY47687.1};
GN   Name=trxB_1 {ECO:0000313|EMBL:SFY47687.1};
GN   ORFNames=STEPF1_00898 {ECO:0000313|EMBL:SFY47687.1};
OS   Streptomyces sp. F-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY47687.1, ECO:0000313|Proteomes:UP000095403};
RN   [1] {ECO:0000313|EMBL:SFY47687.1, ECO:0000313|Proteomes:UP000095403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY47687.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000849};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FKJI03000002; SFY47687.1; -; Genomic_DNA.
DR   RefSeq; WP_070026528.1; NZ_FKJI03000002.1.
DR   AlphaFoldDB; A0A1K2FKX3; -.
DR   OrthoDB; 9786503at2; -.
DR   Proteomes; UP000095403; Unassembled WGS sequence.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 1.
DR   Pfam; PF07992; Pyr_redox_2; 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,
KW   ECO:0000313|EMBL:SFY47687.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095403}.
FT   DOMAIN          6..281
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   311 AA;  33135 MW;  563FD358EC901874 CRC64;
     MDTQLYDTVI VGGGPAGLNG ALYLGRSRRR VLLVDSGDAR NMAAGVMHNV LTNDGAAIAD
     FRARARAQLA SYDVTFRDDE VVSAESGGDH VVVTAKESGT VRARTLLYAA GVRSVLPPVP
     GLAPLWGKAV FECPYCHAWE VRERRFAVYG GGVPSECLAS TLTVWSDDIT YLAGGRALPA
     DEQDRLAAAK VPVLTEGVRE LRPHPEGLEV VFADGRTASY GAMFLHLDIE PRVAPLRPWL
     TAPDLESVQT DDRGRTSLPR LYVAGDLGRN MQQAAMAAAS GGLAAMAINA DLIREDRPGS
     LPEPPPPAPA R
//