ID   TRXB_MYCPN              Reviewed;         315 AA.
AC   P75531;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=MPN_240; ORFNames=MP591;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=9202470; DOI=10.1099/00221287-143-6-1933;
RA   Ben-Menachem G., Himmelreich R., Herrmann R., Aharonowitz Y., Rottem S.;
RT   "The thioredoxin reductase system of mycoplasmas.";
RL   Microbiology 143:1933-1940(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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}.
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; U51988; AAC45451.1; -; Genomic_DNA.
DR   EMBL; U00089; AAB96239.1; -; Genomic_DNA.
DR   PIR; S73917; S73917.
DR   RefSeq; NP_109928.1; NC_000912.1.
DR   RefSeq; WP_010874597.1; NC_000912.1.
DR   AlphaFoldDB; P75531; -.
DR   SMR; P75531; -.
DR   STRING; 272634.MPN_240; -.
DR   EnsemblBacteria; AAB96239; AAB96239; MPN_240.
DR   KEGG; mpn:MPN_240; -.
DR   PATRIC; fig|272634.6.peg.259; -.
DR   HOGENOM; CLU_031864_5_3_14; -.
DR   OMA; VDNFPGY; -.
DR   BioCyc; MetaCyc:MON-543; -.
DR   BioCyc; MPNE272634:G1GJ3-381-MON; -.
DR   Proteomes; UP000000808; 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..315
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166738"
FT   BINDING         45..52
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        145..148
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   315 AA;  34532 MW;  7155E4AF8D2A2EE7 CRC64;
     MLKVKSDFLT KDQVIYDVAI VGAGPAGIAA GIYGKRANLN LAIIEGSTPG GKVVKTNIVE
     NYPGYKSITG PDLGLEMYNH LIDLEPTFFY ANLIKLDKAA DTFILYLDDK TVVFAKTVIY
     ATGMLERKLG VAKEDHFYGK GISYCAICDG SLYKDQVVGV VGGGNSAIQE ALYLASMAKT
     VHLIHRREGF RADETALNKL RNLPNVVFHL NYTVKELLGN NTLNGIVLQN TLDHSTKQID
     LNCVFPYIGF ESITKPVEHL NLKLDPQGFL ITNEQMETSL KGLFAAGDCR SKHFRQIGTA
     INDGIIAVLT IRDVL