ID TRXB_ALIFS Reviewed; 45 AA. AC P80892; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 09-APR-2025, entry version 94. DE RecName: Full=Thioredoxin reductase; DE Short=TRXR; DE EC=1.8.1.9; DE Flags: Fragment; GN Name=trxB; OS Aliivibrio fischeri (Vibrio fischeri). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Aliivibrio. OX NCBI_TaxID=668; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=ATCC 33715 / Y-1; RX PubMed=9183020; DOI=10.1111/j.1432-1033.1997.00790.x; RA Petushkov V.N., Lee J.; RT "Purification and characterization of flavoproteins and cytochromes from RT the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1."; RL Eur. J. Biochem. 245:790-796(1997). 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 -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P0A9P4}; CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. 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 AlphaFoldDB; P80892; -. DR SMR; P80892; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADPH) activity; IEA:UniProtKB-EC. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR InterPro; IPR003953; FAD-dep_OxRdtase_2_FAD-bd. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR Pfam; PF00890; FAD_binding_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; NADP; KW Oxidoreductase; Redox-active center. FT CHAIN 1..>45 FT /note="Thioredoxin reductase" FT /id="PRO_0000166757" FT BINDING 35..42 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT NON_TER 45 SQ SEQUENCE 45 AA; 4658 MW; D0696133DE491602 CRC64; MNVKHSKLLI LGSGPAGYTA AVYAARANLN PVMITGMQQG GQLTN //