ID   TRXB_BORBU              Reviewed;         326 AA.
AC   P94284; O51467;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=BB_0515;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA   Barbour A.G., Hinnebusch J.;
RT   "Phenylalanyl-tRNA synthetase genes (alpha and beta subunits) and
RT   thioredoxin reductase gene of Borrelia burgdorferi.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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 {ECO:0000250}.
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; U82978; AAB41020.1; -; Genomic_DNA.
DR   EMBL; AE000783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B70164; B70164.
DR   RefSeq; WP_002656440.1; NC_001318.1.
DR   RefSeq; YP_008686580.1; NC_001318.1.
DR   AlphaFoldDB; P94284; -.
DR   SMR; P94284; -.
DR   PRIDE; P94284; -.
DR   PATRIC; fig|224326.49.peg.906; -.
DR   OMA; VDNFPGY; -.
DR   Proteomes; UP000001807; 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; Reference proteome.
FT   CHAIN           1..326
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166720"
FT   BINDING         55..62
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         298..307
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   DISULFID        156..159
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   CONFLICT        303
FT                   /note="L -> P (in Ref. 1; AAB41020)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315..326
FT                   /note="FIASVELGNFLK -> LLHLLS (in Ref. 1; AAB41020)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  35673 MW;  E0F5AC6ACFFFFF3B CRC64;
     MLEFETIDIN LTKKKNLSQK EVDFIEDVII VGSGPAGLTA GIYSVMSNYK AAILEGPEPG
     GQLTTTTEVY NYPGFKNGIS GRNLMLNMRE QVVNLGAKTF PETVFSIKRK GNIFYLYTEN
     YIYKSKAVII AVGSKPKKLE TLKNSGLFWN KGISVCAICD GHLFKGKRVA VIGGGNTALS
     ESIYLSKLVD KVYLIVRKNN LRAIAMLRDS VAKLPNIEIL YNSEAIEVDG KSSVSSVKIF
     NKKDNVVYEL EVSAVFMAVG YKPNTEFLKG FLDLDEEGFI VTKDVVKTSV DGVFSCGDVS
     NKLYAQAITA AAEGFIASVE LGNFLK