ID TRXB_STRCO Reviewed; 322 AA. AC P52215; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 151. DE RecName: Full=Thioredoxin reductase; DE Short=TRXR; DE EC=1.8.1.9 {ECO:0000250|UniProtKB:P9WHH1}; GN Name=trxB {ECO:0000303|PubMed:9795152}; OrderedLocusNames=SCO3890; GN ORFNames=SCH24.12c; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=9795152; DOI=10.1016/s0378-1119(98)00357-6; RA Gal-Mor O., Borovok I., Av-Gay Y., Cohen G., Aharonowitz Y.; RT "Gene organization in the trxA/B-oriC region of the Streptomyces coelicolor RT chromosome and comparison with other eubacteria."; RL Gene 217:83-90(1998). RN [2] RP SEQUENCE REVISION. RA Aharonowitz Y.; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). RN [4] RP INDUCTION. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=9755177; DOI=10.1093/emboj/17.19.5776; RA Paget M.S., Kang J.G., Roe J.H., Buttner M.J.; RT "sigmaR, an RNA polymerase sigma factor that modulates expression of the RT thioredoxin system in response to oxidative stress in Streptomyces RT coelicolor A3(2)."; RL EMBO J. 17:5776-5782(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + CC NADPH + H(+); 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:0000250|UniProtKB:P9WHH1}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P9WHH1}; CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P9WHH1}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WHH1}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- INDUCTION: Expressed from 2 promoters, 1 of which (trxBp1) is under CC control of SigR, and further transiently induced (about 50-fold) by the CC thiol-oxidizing agent diamide. Part of the trxB-trxA operon. CC {ECO:0000269|PubMed:9755177}. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000250|UniProtKB:P9WHH1}. CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000305}. 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; X92105; CAA63076.1; -; Genomic_DNA. DR EMBL; X92104; CAA63075.1; -; Genomic_DNA. DR EMBL; AJ007313; CAA07451.1; -; Genomic_DNA. DR EMBL; AL939118; CAB42713.1; -; Genomic_DNA. DR PIR; T36577; T36577. DR PIR; T42062; T42062. DR AlphaFoldDB; P52215; -. DR SMR; P52215; -. DR FunCoup; P52215; 336. DR STRING; 100226.gene:17761517; -. DR PaxDb; 100226-gene:17761517; -. DR KEGG; sco:SCO3890; -. DR PATRIC; fig|100226.15.peg.3963; -. DR eggNOG; COG0492; Bacteria. DR HOGENOM; CLU_031864_5_1_11; -. DR InParanoid; P52215; -. DR OMA; AACKYIC; -. DR OrthoDB; 9806179at2; -. DR PhylomeDB; P52215; -. DR Proteomes; UP000001973; Chromosome. DR AbasyAtlas; P52215; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADPH) activity; ISS:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central. DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro. 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 InterPro; IPR050097; Ferredoxin-NADP_redctase-like. DR InterPro; IPR008255; PNDR_II_active_site. DR InterPro; IPR005982; Thioredox_Rdtase. DR NCBIfam; TIGR01292; TRX_reduct; 1. DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 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. DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase; KW Redox-active center; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..322 FT /note="Thioredoxin reductase" FT /id="PRO_0000166753" FT BINDING 12..15 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 34..42 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 51 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 84 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 176 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 182 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 239 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 259 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 279 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 286..289 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT BINDING 286 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT DISULFID 136..139 FT /note="Redox-active" FT /evidence="ECO:0000250|UniProtKB:P9WHH1" FT CONFLICT 26 FT /note="A -> R (in Ref. 1; CAA63075/CAA07451)" FT /evidence="ECO:0000305" FT CONFLICT 73..74 FT /note="ER -> DG (in Ref. 1; CAA63075/CAA07451)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="Missing (in Ref. 1; CAA63075)" FT /evidence="ECO:0000305" FT CONFLICT 234 FT /note="G -> A (in Ref. 1; CAA63075)" FT /evidence="ECO:0000305" FT CONFLICT 258 FT /note="Missing (in Ref. 1; CAA63075)" FT /evidence="ECO:0000305" FT CONFLICT 300 FT /note="V -> L (in Ref. 3; CAB42713)" FT /evidence="ECO:0000305" FT CONFLICT 304 FT /note="P -> R (in Ref. 3; CAB42713)" FT /evidence="ECO:0000305" SQ SEQUENCE 322 AA; 34156 MW; 1B337B1742E3C457 CRC64; MSDVRNVIII GSGPAGYTAA LYTARASLKP LVFEGAVTAG GALMNTTEVE NFPGFQDGIM GPELMDNMRA QAERFGAELI PDDVVAVDLS GEIKTVTDTA GTVHRAKAVI VTTGSQHRKL GLPNEDALSG RGVSWCATCD GFFFKDQDIA VIGGGDTAME EATFLSRFAK SVTIVHRRDT LRASKAMQER AFADPKISFV WDSEVAEVQG DQKLAGLKLR NVKTGELSDL PVTGLFIAIG HDPRTELFKG QLDLDPEGYL KVDAPSTRTN LTGVFGAGDV VDHTYRQAIT AAGTGCSAAV DAEPFLAALS DEDKAEPEKT AV //