ID   TRXB_AQUAE              Reviewed;         323 AA.
AC   O66790;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 69.
DE   RecName: Full=Thioredoxin reductase;
DE            Short=TRXR;
DE            EC=1.8.1.9;
GN   Name=trxB; OrderedLocusNames=aq_500;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(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.
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DR   EMBL; AE000657; AAC06756.1; -; Genomic_DNA.
DR   PIR; B70345; B70345.
DR   RefSeq; NP_213350.1; -.
DR   HSSP; P09625; 1TDE.
DR   GeneID; 1193208; -.
DR   GenomeReviews; AE000657_GR; aq_500.
DR   KEGG; aae:aq_500; -.
DR   NMPDR; fig|224324.1.peg.365; -.
DR   HOGENOM; O66790; -.
DR   OMA; O66790; IGDIRNT.
DR   BioCyc; AAEO224324:AQ_500-MON; -.
DR   BRENDA; 1.8.1.9; 189781.
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    323       Thioredoxin reductase.
FT                                /FTId=PRO_0000166718.
FT   NP_BIND      42     49       FAD (By similarity).
FT   NP_BIND     286    295       FAD (By similarity).
FT   DISULFID    143    146       Redox-active (By similarity).
SQ   SEQUENCE   323 AA;  35101 MW;  363FC62EFDD03328 CRC64;
     MAVSLMQQPD KVYDVIIIGA GPAGTTAAIY TARAGWKTLV LYRAEADGAL GVTQKIENYP
     GVPGPLSGYE LLKIMREQAK SFGAEFVRGK VIATDLNSDP KKVYTIDGRE FRGKTIIVAS
     GAMERANKFK GEEEFLGRGV SYCGVCDAAF FKDQPVAVIG DDDYAIEEAE FIARFANKVF
     FVVPGSKIKA PPEVIEHFEK LPNVEILLRH RPIEIVGDQV VKGIKLKDLE KKEEKLLEVN
     GVFIFLGGTK PSVDFLMGQV EMTEGDCIVV NEEMMTSVPG VFAAGDVLCN EVKQAVVAAA
     MGCKAALAVD KFLSGKKKIV PQW
//