ID   TRXB_MYCPU              Reviewed;         307 AA.
AC   Q98PK9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=MYPU_7130;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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; AL445565; CAC13886.1; -; Genomic_DNA.
DR   PIR; A99601; A99601.
DR   RefSeq; WP_010925514.1; NC_002771.1.
DR   AlphaFoldDB; Q98PK9; -.
DR   SMR; Q98PK9; -.
DR   STRING; 272635.MYPU_7130; -.
DR   PRIDE; Q98PK9; -.
DR   EnsemblBacteria; CAC13886; CAC13886; CAC13886.
DR   KEGG; mpu:MYPU_7130; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_3_14; -.
DR   OMA; VDNFPGY; -.
DR   OrthoDB; 692968at2; -.
DR   BioCyc; MPUL272635:G1GT6-726-MON; -.
DR   Proteomes; UP000000528; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC.
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   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 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..307
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166739"
FT   BINDING         36..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         278..287
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   DISULFID        138..141
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   307 AA;  33456 MW;  04A0F5ED4DA28D97 CRC64;
     MSQNKIYDVA IIGAGPGALT AAIYTSRGNL DTVFIDNAAP GGKLIYASKI ENWPGDTIVK
     GTDLAIRFFE HAQAFGAKYE YGKVVDLINI KDDLKELVLE DGKKIQAKSV IIASGMVSRK
     PREILNYDEF ENRGVSYCVI CDGPMYGHNP AIIIGGGNSA VEEGTFLSSI ASKVYVIVRD
     SDFIAEKALV NDLKSRKNIE VLFNASVKEL HGKDALEYAI VNHNGKEVKL EVASLFPYIG
     FLPSAEYAKN AGVLEPNGFI KTDEFMETKV PGIYAIGDIR IKDIRQILTA TSDGTIAGKI
     LTNRIKK