ID   TRXB_UREPA              Reviewed;         309 AA.
AC   Q9PR71;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   10-JUN-2026, entry version 128.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=UU074;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
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 {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; AF222894; AAF30479.1; -; Genomic_DNA.
DR   RefSeq; WP_006688550.1; NC_002162.1.
DR   AlphaFoldDB; Q9PR71; -.
DR   SMR; Q9PR71; -.
DR   STRING; 273119.UU074; -.
DR   EnsemblBacteria; AAF30479; AAF30479; UU074.
DR   GeneID; 29672186; -.
DR   KEGG; uur:UU074; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_3_14; -.
DR   OrthoDB; 9806179at2; -.
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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR050097; Ferredoxin-NADP_redctase_2.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..309
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166755"
FT   BINDING         35..42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         277..286
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   DISULFID        134..137
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
SQ   SEQUENCE   309 AA;  34150 MW;  CC01383CD53CB8A4 CRC64;
     MNQEVYDLVI IGAGPAGLAA AVYAKRSGLN VIIVEKQFPG GKIALTSNVE NYLGINSIPG
     PELAYKMYEQ VLNLNVSIIY EAADEISLKE KYKKIKLTTQ TLITKTVIIA TGTENRRLNI
     LGELEFENKG ISYCAICDGP LYKNKAVSVI GSGNSAVEEA IYLATIAKEV HLIANKPQFK
     AEQQLVQIAN NTPNIKIYYN KQTFEFFGHQ FLEGLKFRDL ITNEVTTLNI EANFTFIGLL
     PSRINTNNLC IFNEVNGFIT TDKNMQTSVC GIFAAGDIVD KNVRQIATAT NDGVIAALYA
     KEYITRNNW
//