ID   TRXB_CHLTR              Reviewed;         312 AA.
AC   O84101;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=CT_099;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
CC       + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE001273; AAC67690.1; ALT_INIT; Genomic_DNA.
DR   PIR; B71556; B71556.
DR   RefSeq; NP_219602.1; -.
DR   HSSP; Q39243; 1VDC.
DR   PHCI-2DPAGE; O84101; -.
DR   GeneID; 884181; -.
DR   GenomeReviews; AE001273_GR; CT_099.
DR   KEGG; ctr:CT099; -.
DR   HOGENOM; O84101; -.
DR   BioCyc; CTRA315277:CT099-MON; -.
DR   BRENDA; 1.8.1.9; 108.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN         1    312       Thioredoxin reductase.
FT                                /FTId=PRO_0000166726.
FT   NP_BIND      33     43       FAD (By similarity).
FT   NP_BIND     283    292       FAD (By similarity).
FT   DISULFID    138    141       Redox-active (By similarity).
SQ   SEQUENCE   312 AA;  33508 MW;  729D0D22F8FA0A39 CRC64;
     MTHAKLVIIG SGPAGYTAAI YASRALLTPV LFEGFFSGIA GGQLMTTTEV ENFPGFPEGV
     LGHQLMDLMK TQAQRFGTQV LSKDITAVDF SVRPFVLKSG KETFTCDACI IATGASAKRL
     SIPGAGDNEF WQKGVTACAV CDGASPIFRD KDLFVVGGGD SALEEAMFLT RYGKRVFVVH
     RRDTLRASKV MVNKAQANEK IFFLWNSEIV KISGDTLVRS IDIYNNVDET TTTMEAAGVF
     FAIGHQPNTA FLGGQVALDE NGYIITEKGS SRTSVPGVFA AGDVQDKYYR QAITSAGSGC
     MAALDAERFL EN
//