ID   TRXB_BUCAP              Reviewed;         319 AA.
AC   P81433;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=BUsg_304;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Thao M.L., Baumann P.;
RT   "Nucleotide sequence of a DNA fragment from Buchnera aphidicola (Aphid
RT   endosymbiont) containing the genes aspS-trxB-serS-serC-aroA-rpsA-himD-
RT   tpiA.";
RL   Curr. Microbiol. 35:68-69(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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   -!- 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}.
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DR   EMBL; L43549; AAC05433.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM67858.1; -; Genomic_DNA.
DR   RefSeq; WP_011053825.1; NC_004061.1.
DR   AlphaFoldDB; P81433; -.
DR   SMR; P81433; -.
DR   STRING; 198804.BUsg_304; -.
DR   EnsemblBacteria; AAM67858; AAM67858; BUsg_304.
DR   KEGG; bas:BUsg_304; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_1_6; -.
DR   OMA; VDNFPGY; -.
DR   OrthoDB; 692968at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..319
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166722"
FT   BINDING         36..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         288..297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   DISULFID        136..139
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   319 AA;  35543 MW;  BB1A774645BCDBAD CRC64;
     MELKNHKKII ILGSGPAGYT AAIYSSRANL NPLLITGINK GGQLMNTNEI ENWPGDFKKI
     TGPELMNRMH EHSLKFKTEI VYDNIISVEF KKKPFFLLGE YNKYTCDAVI IATGANPRYL
     GLSSENKFKG KGISTCAVCD GFFYKNKEIA VVGGGNTAIE ETLYLSNFVK KIYLIHRRNN
     FKAEKILIDR LLKIVKTKKV ILHLNSTIED ILGNNKGVTH LLIKNKNLKE KKKLKIAVSG
     LFVAIGYIPN TDIFTDQLKM KDGYIKIKKG THGNYTQTNI PGVFAAGDVI DHVYRQAITS
     SASGCMAALD SERYLNSLS