ID   TRXB_CHLMU              Reviewed;         312 AA.
AC   Q9PKT7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=TC_0375;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39233.1; -; Genomic_DNA.
DR   PIR; C81710; C81710.
DR   RefSeq; WP_010230279.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKT7; -.
DR   SMR; Q9PKT7; -.
DR   STRING; 243161.TC_0375; -.
DR   EnsemblBacteria; AAF39233; AAF39233; TC_0375.
DR   GeneID; 1245727; -.
DR   KEGG; cmu:TC_0375; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_1_0; -.
DR   OMA; VDNFPGY; -.
DR   OrthoDB; 692968at2; -.
DR   Proteomes; UP000000800; 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..312
FT                   /note="Thioredoxin reductase"
FT                   /id="PRO_0000166724"
FT   BINDING         33..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT   BINDING         283..292
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   312 AA;  33556 MW;  53824B207C24158D CRC64;
     MTHVKLAIIG SGPAGYTAAI YASRALLTPI LFEGFFSGIA GGQLMTTTEV ENFPGFPQGV
     LGHQLMENMK MQAQRFGTQV IAKDITSVDF SVRPFVLKSG EDTFTCDACI IATGASAKRL
     SIPGAGDNEF WQKGVTACAV CDGASPIFRD RDLFVIGGGD SALEEAMFLT RYGKRVFVVH
     RRDTLRASKA MVNKAQANEK IVFLWNSEVV KILGDSLVRS IDIFNNVEKT TVTMEAAGVF
     FAIGHQPNTA FLGGQLSLDE NGYIITEKGS SRTSVPGVFA AGDVQDKYYR QAITSAGSGC
     MAALDAERFL EK